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1Brilliant III Ultra-Fast SYBR ® GreenQPCR Master MixQuick Reference Guide for the AgilentMx3000P/Mx3005P QPCR SystemsAgilent Technologies This quick reference guide provides an optimized protocol for usingAgilent’s Brilliant III Ultra-Fast SYBR® Green QPCR Master Mix with the Mx3000P and Mx3005P QPCR Systems. For detailed instructions, refer to the full product manual.Prepare theReactions 1Dilute the reference dye 1:500 using nuclease-free PCR-grade water.2Prepare the experimental reactions by combining the components of thereagent mixture in the order listed in the table below. Prepare a singlereagent mixture for replicate reactions (plus at least one reactionvolume excess) using multiples of each component.3Gently mix the reagent mixture without creating bubbles, thendistribute the mixture to the experimental reaction tubes.4Add x μl of experimental DNA to each reaction to bring the finalreaction volume to 20 μl. The table below lists a suggested quantityrange for different DNA templates.*Refers to RNA input amount during cDNA synthesis5Mix the reactions without creating bubbles, then centrifuge briefly.Reagent MixtureNuclease-free PCR-grade water to bring final volume to 20 μl (including DNA)10 μl of 2× SYBR Green QPCR Master Mixx μl of upstream primer at optimized concentration (200–500 nM)x μl of downstream primer at optimized concentration (200–500 nM)0.3 μl of diluted reference dyeDNA Quantity per reactionGenomic DNA 5 pg – 50 ngcDNA 0.5 pg – 100 ng*2Brilliant III Ultra-Fast SYBR® Green QPCR Master MixSet Up theQPCR Plate andThermal Profile 1Complete the Plate Setup screen for a new experiment as needed, including assigning well types and assay information.2On the Thermal Profile Setup screen, set the Thermal Profile Designselection to Standard .•Under Pre-Melt/RT Segment , click 1 Plateau .•Under Amplification Segment , click Fast 2 Step .•Under Dissociation/Melt Segment , click Dissociation/Melt .3Adjust the thermal profile according to the image below. The profileincludes a 5-second denaturation step. Note that some assays mayrequire a denaturation of up to 20 seconds. The exact denaturation timeneeds to be optimized for each target. Run the PCRProgram1Place the reactions in the Mx3000P/Mx3005P instrument.2On the Run screen, click Start Run .Analyze Data 1Analyze the results of the run as needed for your experiment.Notice to Purchaser: Purchase of this product includes an immunity from suit under patents specified in the product insert to use only the amount purchased for the purchaser’s own internal research. No other patent rights are conveyed expressly, by implication, or by estoppel. Further information on purchasing licenses may be obtained by contacting the Director of Licensing, Applied Biosystems, 850 Lincoln Centre Drive, Foster City, California 94404, USA.SYBR ® is licensed for research and development only under patents and patent applications owned by Invitrogen Corporation.SYBR ® is a registered trademark of Molecular Probes, Inc .Manual Part Number 5990-7205, Revision B0For Research Use Only. Not for use in diagnostic procedures.©Agilent Technologies, Inc. 2015, 2016PR7000-04505990-5995EN Product InformationCatalog #600882, 400 reactionsCatalog #600883, 4000 reactions Ordering Information By phone (US and Canada*): 800-227-9770On the web: /genomicsTechnical Services By phone (US and Canada*): 800-227-9770Byemail:*************************For other countries, please contact your local sales representative at /genomics/contactusAgilent Technologies。
RFQ冷却聚束器RFQ1L的研制的开题报告一、项目简介本项目主要研发一种冷却聚束器RFQ1L，该聚束器具有高加速梯度和较高的输运效率，可广泛应用于各种离子加速器中。
本项目将开发新型材料和工艺，提高制造工艺水平和生产效率，从而实现高品质和高性能的聚束器。
二、项目背景和意义RFQ聚束器是一种可以将相对大量的离子加速到高能量的设备，广泛应用于医学放射学、核园艺学、超导材料等领域。
而传统的空间加速器中的聚束器存在造成高达20%的离子束损失的问题，这不仅会导致加速器效率的下降，也会增加用于冷却的氦气的消耗。
本项目旨在通过采用新的材料和工艺，设计一款高效率、低损失的冷却聚束器RFQ1L，以提高加速器的能效和降低运行成本。
三、项目技术路线本项目受到加速器技术、电子学、沉积物工程、材料学和制造工艺等多个方面的影响。
1.设计阶段。
首先，对RFQ聚束器进行研究和分析，以确定冷却聚束器RFQ1L 的设计要求；然后，采用软件工具进行3D设计和仿真分析，优化设计，确定RFQ1L 的尺寸和形状，最终形成初步设计方案。
2.材料研发阶段。
开发新型材料，具备更好的导电性，热导性和机械性能，以提高聚束器的效率和稳定性。
3.制造工艺研发阶段。
采用复合材料制造技术，提高制造效率和制造工艺水平，降低制造成本。
四、项目成果本项目将重点实现以下成果：1.确定冷却聚束器RFQ1L的设计要求和方案；2.开发新型材料；3.制造出高效率、低损失的RFQ1L。
五、项目进度安排本项目的总工期为24个月，初步进度安排如下：1.设计阶段：2个月2.材料研发阶段：8个月3.制造工艺研发阶段：12个月4.实验性能测试：2个月六、预计经费支出本项目的预计经费支出为100万美元，主要用于材料研发、制造工艺研发和实验性能测试等方面。
具体的经费支出细节将在项目启动后进行进一步的确认和制定。
七、项目团队本项目的团队将由专业的研究人员和技术工程师组成，他们在材料学、制造工艺和加速器技术领域具有相当的经验和知识。
THE NEEDSEvides Waterbedrijf required measurement of turbidity and flow to monitor water quality in the distribution network and manage the network. Until recently, this data had been recorded manually and analysed with outdated equipment. This process no longer fitted with the strategic pillar “digitising primary processes” which was an important aim of the Netherlands water provider. Evides Waterbedrijf developed an all-in-one measuring device which allowed them to make all distribution network measurements. During the measurement process, turbidity, flow and GPS location were all recorded and logged in real-time from the field. This data could be used to determine water quality of the distribution network, assess the effectiveness of previously implemented drainage actions and continue to optimise drainage plans. The process being largely automated. The flow meter was part of the total standpipe solution which was lightweight and easy to dismantle in the field.THE SOLUTIONTo support the needs of EvidesWaterbedrijf, Honeywell Smart Energyoffered their Q4000 electromagneticmeter as part of the standpipe solution.Featuring high quality design andengineering, Honeywell’s Q4000electromagnetic water meter is builtfor maintaining highly accurateperformance and lasting durabilityin demanding environments.With an unrestricted flow tube with nomoving parts and a 10-year batterylife, the Q4000 offers unrivalledperformance for an electromagneticwater meter. Delivering consistentaccuracy over a wide flow-ratemeasuring range, the meter can beadapted to suit either predominantlyhigh or low flow rates, and is ideal fordistribution network applications.The Q4000 is a high-performingelectromagnetic meter, ideal for networkmanagement and leakage monitoring.HON EYWELL’SW A TER M ETERCase StudySupports Accurate Real-Time Distribution Network AnalysisGood quality water supply is provided for the entire population in the Netherlands. Water consumption is one of the lowest in developed countries at 128 litres per capita per day and water leakage in the distribution network is one of the lowest in the world at only 6%.The Q4000 water meter forms part of the total standpipe solution.The Q4000 from Honeywell Smart Energy is a high-performing electromagnetic meter, ideal for bulk flow metering applications such as network management and leakage monitoring.-It has a fast continuous sampling rate, providing highly accurate and reliable measurement.-The Q4000’s extremely tough stainless steel constructionensures a long working life, while its lightweight body makes storage, transportation and installation both simpler and safer.-With an unrestricted flow tube, the Q4000 ensures minimal pressureABOUT EVIDES WATERBEDRIJFEvides Waterbedrijf supplies safe and clean drinking water 24 hours a day, 365 days a year to 2.5 millioncustomers and the business community in Zeeland, in the South West of Holland and the Brabantse Wal.Additionally, Evides Waterbedrijf offers tailor-made industrial water services to large industrial customers in the Netherlands, Belgium and Germany.THE BENEFITSloss, even at the highest flowrates, resulting in reduced network system pressures, helping to prevent leakage from burst pipes. -A large, bright and easy-to-read LCD, showing volume and instantaneous flow rate, is ideal for real-time network control and water management. -With the Q4000’s 10-yearcontinuous battery life and no need for calibration, expensive regular maintenance is a thing of the past. -With bi-directional pulse outputs, the Q4000 provides dependable connectivity to critical water management systems including AMR and data logging devices.All rights reserved.The company’s policy is one of continuous product improvement and the right is reserved to modify the specifications contained herein without notice. These products have been manufactured with current technology and in accordance with the applicable referenced standards.SS-20-2 ENG | 02/20© 2020 Honeywell International Inc.For more informationElster Water Metering Ltd130 Camford Way Sundon Park, Luton Bedfordshire, LU3 3AN United Kingdom T +44 1582 846400F +44 1582 564728*************************。
GE HealthcareInstructions 71-5027-68 AH HisTrap affinity columns HisTrap HP, 1 ml and 5 mlHisTrap™ HP is a ready to use column, prepacked with precharged Ni Sepharose™ High Performance. This prepacked column is ideal for preparative purification of Histidine-tagged recombinant proteins by immobilized metal ion affinity chromatography (IMAC).The special design of the column, together with the high-performance matrix of the Ni Sepharose medium, provides fast, simple, and easy separations in a convenient format.Ni Sepharose High Performance has low nickel (Ni2+) ion leakage and is compatible with a wide range of additives used in protein purification. HP columns can be operated with a syringe, peristaltic pump, or liquid chromatography system such as ÄKTA™ design chromatography systems.CAUTION! Contains nickel. May produce an allergic reaction..1Pack size available by special order.Connector kit1Union 1/16” female/M6 male is also needed.2Union M6 female/1/16” male is also needed.Table of contents1.Description..............................................................................32.General considerations.....................................................63.Operation.................................................................................74.Optimization........................................................................115.Stripping and recharging..............................................126.Cleaning-in-place.............................................................137.Scaling-up............................................................................138.Storage..................................................................................149.Troubleshooting................................................................1410.Intended use.......................................................................1711.Ordering Information (18)Code No. Product No. supplied 17-5247-01 HisTrap HP 5 × 1 ml 17-5247-05 HisTrap HP 100 × 1 ml 117-5248-01 HisTrap HP 1 × 5 ml 17-5248-02 HisTrap HP 5 × 5 ml 17-5248-05HisTrap HP 100 × 5 ml 1Connectors supplied Usage No. supplied 1/16” male/luer femaleConnection of syringe to top of HiTrap column1Tubing connector flangeless/M6 femaleConnection of tubing (e.g. Peristaltic Pump P1) to bottom of HiTrap column 11Tubing connector flangeless/M6 male Connection of tubing (e.g. Peristaltic Pump P1) to top of HiTrap column 21Union 1/16” female/M6 male Connection to original FPLC™ System through bottom of HiTrap column1Union M6 female/1/16” maleConnection to original FPLC System through top of HiTrap column 1Stop plug female, 1/16”Sealing bottom of HiTrap column 2, 5 or 71DescriptionMedium propertiesHisTrap HP 1 ml and 5 ml columns are prepacked with NiSepharose High Performance, which consists of 34 µm highlycross-linked agarose beads with an immobilized chelating group.The medium has then been charged with Ni2+-ions.Several amino acids, for example histidine, form complexes with many metal ions. Ni Sepharose High Performance selectively binds proteins if suitable complex-forming amino acid residues areexposed on the protein surface.Additional histidines, such as in the case of (histidine)6 -tag,increase affinity for Ni2+ and generally make the histidine-tagged protein the strongest binder among other proteins in for example an E. coli extract.Column propertiesHisTrap HP columns are made of biocompatible polypropylenethat does not interact with biomolecules. Columns are deliveredwith a stopper on the inlet and a snap-off end on the outlet. Thecolumns have porous top and bottom frits that allow high flowrates. They cannot be opened or refilled.Columns can be operated with either a syringe and the supplied luer connector, a peristaltic pump, or a chromatography systemsuch as ÄKTA design.Note:To prevent leakage, ensure that the connector is tight.Table 1. HisTrap HP characteristics.1Dynamic binding capacity conditions:Note: Dynamic binding capacity is protein-dependent.2H 2O at room temperature 3Ni 2+-stripped mediumMatrixHighly cross-linked spherical agarose, 6%Average particle size 34 µmMetal ion capacity ~ 15 µmol Ni 2+/ml mediumDynamic binding capacity 1 At least 40 mg (histidine)6-tagged protein/ml medium Column volumes 1 ml or 5 ml Column dimensions i.d. × H:0.7 × 2.5 cm (1 ml) 1.6 × 2.5 cm (5 ml)Recommended flow rate 1 and 5 ml/min for 1 and 5 ml column respectivelyMax. flow rates 4 and 20 ml/min for 1 and 5 ml column respectively Max back pressure 20.3 MPa, 3 barCompatibility during use Stable in all commonly used buffers, reducingagents, denaturants, and detergents (s ee Table 2)Chemical stability 30.01 M HCl, 0.1 M NaOH. Tested for 1 week at 40°C.1 M NaOH, 70% acetic acid. Tested for 12 hours.2% SDS. Tested for 1 hour.30% 2-propanol. Tested for 30 min.Avoid in buffers Chelating agents, e.g. EDTA, EGTA, citrate (see Table 2)pH stability 3short term (at least 2 hours): 2 to 14 long term (≤ 1 week): 3 to 12Storage 20% ethanol Storage temperature4°C to 30°CSample:1 mg/ml (histidine)6-tagged pure protein (M r 28 000 or 43 000) inbinding buffer (Q B, 10% determination) or (histidine)6-tagged protein bound from E. coli extractColumn volume: 0.25 ml or 1 ml Flow rate: 0.25 ml/min or 1 ml/min Binding buffer: 20 mM sodium phosphate, 0.5 M NaCl, 5 mM imidazole, pH 7.4Elution buffer: 20 mM sodium phosphate, 0.5 M NaCl, 0.5 M imidazole, pH 7.4The Ni 2+-charged medium is compatible with all commonly used aqueous buffers, reducing agents, denaturants such as 6 M Gua-HCl and 8 M urea, and a range of other additives (see Table 2).Table 2. Ni Sepharose High Performance is compatible with the following compounds, at least at the concentrations given.1See Notes and blank run, p. 10–11.2Tested for 1 week at 40°C.3The strong chelator EDTA has been used successfully in some cases, at 1 mM.Generally, chelating agents should be used with caution (and only in the sample, not the buffers). Any metal-ion stripping may be counteracted by addition of a small excess of MgCl 2 before centrifugation/filtration of the sample. Note that stripping effects may vary with applied sample volume.Reducing agents 15 mM DTE 5 mM DTT20 mM ß-mercaptoethanol 5 mM TCEP10 mM reduced glutathione Denaturing agents 8 M urea 26 M guanidine hydrochloride 2Detergents2% Triton™ X-100 (nonionic)2% Tween™ 20 (nonionic)2% NP-40 (nonionic)2% cholate (anionic)1% CHAPS (zwitterionic)Other additives500 mM imidazole 20% ethanol 50% glycerol 100 mM Na 2SO 41.5 M NaCl 1 mM EDTA 360 mM citrate 3Buffer substances50 mM sodium phosphate, pH 7.4100 mM Tris-HCl, pH 7.4100 mM Tris-acetate, pH 7.4100 mM HEPES, pH 7.4100 mM MOPS, pH 7.4100 mM sodium acetate, pH 422General considerationsHisTrap HP is supplied precharged with Ni2+ ions. In general, Ni2+ is the preferred metal ion for purification of recombinant histidine-tagged proteins. Note, however, that in some cases it may be wise to test other metal ions, for example Zn2+ and Co2+, as the strength of binding depends on the nature of the histidine-tagged protein as well as the metal ion (see Optimization).We recommend binding at neutral to slightly alkaline pH (pH 7–8) in the presence of 0.5–1.0 M NaCl. Sodium phosphate buffers are often used. Tris-HCl can generally be used, but should be avoided in cases where the metal-protein affinity is very weak, since it may reduce binding strength. Avoid chelating agents such as EDTA or citrate in buffers, see Table2.Including salt, for example 0.5–1.0 M NaCl in the buffers andsamples, eliminates ion-exchange effects but can also have amarginal effect on the retention of proteins.Imidazole at low concentrations is commonly used in the binding and the wash buffers to minimize binding of host cell proteins. For the same reason, it is important to also include imidazole in thesample (generally, at the same concentration as in the washbuffer). At somewhat higher concentrations, imidazole may alsodecrease the binding of histidine-tagged proteins. The imidazole concentration must therefore be optimized to ensure the bestbalance of high purity (low binding of host cell proteins) and high yield (binding of histidine-tagged target protein). This optimalconcentration is different for different histidine-tagged proteins,and is usually slightly higher for Ni Sepharose High Performance than for similar IMAC media on the market (see Data File18-1174-40). Use highly pure imidazole; such imidazole givesessentially no absorbance at 280 nm.As alternatives to imidazole elution, histidine-tagged proteins can be eluted from the medium by several other methods orcombinations of methods – a lowering of pH within the range of2.5–7.5 can be used, for example. At pH values below 4, metal ionswill be stripped off the medium.Note:If the proteins are sensitive to low pH, we recommendcollection of the eluted fractions in tubes containing1 M Tris-HCl, pH 9.0 (60–200 µl/ml fraction) to restore thepH to neutral.Chelating agents such as EGTA or EDTA will also strip metal ionsfrom the medium and thereby cause protein elution, but the target protein pool will then contain Ni2+ ions. In this case, Ni2+ ions can be removed by desalting on a HiTrap™ Desalting, a PD-10 Desalting Column, or HiPrep™ 26/10 Desalting, (see Table3).Leakage of Ni2+ from Ni Sepharose High Performance is very low under all normal conditions, lower than for other IMAC mediatested. For applications where extremely low leakage duringpurification is critical, leakage can be even further reduced byperforming a blank run (see page 11). Likewise, a blank run should also be performed before applying buffers/ samples containingreducing agents (see page 11).Whatever conditions are chosen, HisTrap HP columns can beoperated with a syringe, peristaltic pump, or chromatographysystem.Note:If Peristaltic Pump P-1 is used, the maximum flow rate that can be run on a HisTrap HP 1 ml column is 3 ml/min.3OperationBuffer preparationWater and chemicals used for buffer preparation should be of high purity. Filter buffers through a 0.22 µm or a 0.45 µm filter beforeuse.Use high purity imidazole as this will give very low or noabsorbance at 280 nm.If the recombinant histidine-tagged protein is expressed asinclusion bodies, include 6 M Gua-HCl or 8 M urea in all buffers and sample. On-column refolding of the denatured protein may bepossible.Recommended conditionsSample preparationFor optimal growth, induction, and cell lysis conditions for your recombinant histidine-tagged clones, please refer to established protocols.Adjust the sample to the composition and pH of the binding buffer by: Adding buffer, NaCl, imidazole, and additives fromconcentrated stock solutions; by diluting the sample with binding buffer; or by buffer exchange, (see Table 3). Do not use strong bases or acids for pH-adjustment (precipitation risk). Filter the sample through a 0.22 µm or a 0.45 µm filter and/or centrifuge it immediately before applying it to the column.To prevent the binding of host cell proteins with exposed histidine, it is essential to include imidazole at a low concentration in the sample and binding buffer (see Optimization).Binding buffer: 20 mM sodium phosphate, 0.5 M NaCl,20–40 mM imidazole, pH 7.4 (The optimal imidazole concentration is protein-dependent; 20–40 mM is suitable for many proteins.)Elution buffer:20 mM sodium phosphate, 0.5 M NaCl, 500 mM imidazole, pH 7.4 (The imidazole concentration required for elution is protein-dependent).Table 3. Prepacked columns for desalting and buffer exchangePurification1Fill the syringe or pump tubing with distilled water. Remove the stopper and connect the column to the syringe (use the luerconnector provided), laboratory pump or chromatographysystem tubing “drop-to-drop” to avoid introducing air into thesystem.2Remove the snap-off end at the column outlet.3Wash the column with 3–5 column volumes of distilled water.4Equilibrate the column with at least 5 column volumes of binding buffer. Recommended flow rates are 1 ml/min or5 ml/min for the 1 and 5 ml columns respectively.In some cases a blank run is recommended before finalequilibration/ sample application (see page 11).5Apply the pretreated sample using a syringe or a pump.6Wash with binding buffer until the absorbance reaches a steady baseline (generally, at least 10–15 column volumes).Note:Purification results are improved by using imidazole insample and binding buffer (see Optimization).7Elute with elution buffer using a one-step or linear gradient.Five column volumes are usually sufficient if the protein ofinterest is eluted by a one-step gradient. A shallow gradient, forexample a linear gradient over 20 column volumes or more,may separate proteins with similar binding strengths.Note:If imidazole needs to be removed from the protein, use HiTrap Desalting, a PD-10 Desalting Column, or HiPrep26/10 Desalting depending on the sample volume (seeTable3).Note:Ni Sepharose High Performance is compatible withreducing agents. However, removal of any weakly boundNi2+ ions by performing a blank run without reducingagents (as described on page 11) before applying buffer/sample including reducing agents is recommended. Do notleave HisTrap HP columns with buffers including reducingagents when not in use.Note:Leakage of Ni2+ from Ni Sepharose High Performance is low under all normal conditions. The leakage is lower than forother IMAC media tested (see Data File Ni Sepharose HighPerformance, 18-1174-40). For very critical applications,leakage during purification can be even further diminishedby performing a blank run (as described below) beforeloading sample.Blank run:Use binding buffer and elution buffer without reducing agents.1Wash the column with 5 column volumes of distilled water (to remove the 20% ethanol).2Wash with 5 column volumes of elution buffer.3Equilibrate with 10 column volumes of binding buffer.4OptimizationImidazole at low concentrations is commonly used in the binding and the wash buffers to minimize binding of host cell proteins. For the same reason, it is important to also include imidazole in thesample (generally, at the same concentration as in the washbuffer). At somewhat higher concentrations, imidazole may alsodecrease the binding of histidine-tagged proteins. The imidazole concentration must therefore be optimized to ensure the bestbalance of high purity (low binding of host cell proteins), and high yield (binding of histidine-tagged target protein). This optimalconcentration is different for different histidine-tagged proteins,and is usually slightly higher for Ni Sepharose High Performance than for similar IMAC media on the market (see Data File NiSepharose High Performance, 18-1174-40). Finding the optimalimidazole concentration for a specific histidine-tagged protein is a trial-and-error effort, but 20–40 mM in the binding and washbuffers is a good starting point for many proteins. Use a high purity imidazole, such imidazole gives essentially no absorbance at280 nm.Ni2+ is usually the first choice metal ion for purifying most(histidine)6-tagged recombinant proteins from nontagged host cell proteins, and also the ion most generally used. Nevertheless, it isnot always possible to predict which metal ion will be best for agiven protein. The strength of binding between a protein and ametal ion is affected by several factors, including the length,position, and exposure of the affinity tag on the protein, the type of ion used, and the pH of buffers, so some proteins may be easier to purify with ions other than Ni2+.A quick and efficient way to test this possibility and optimizeseparation conditions is to use HiTrap IMAC HP 1 ml columns,which are packed with IMAC Sepharose High Performance (notcharged with metal ions). Each column can be charged withdifferent metal ions, for example Cu2+, Co2+, Zn2+, Ca2+, or Fe2+.Instructions are included with each column.A study to compare the purification of six (histidine)6-taggedrecombinant proteins, including three variants of maltose-binding protein, with different metal ions has indicated that Ni2+ generally gives best selectivity between (histidine)-tagged and nontaggedhost-cell proteins (see Application Note 18-1145-18).5Stripping and rechargingNote:The column does not have to be stripped and recharged between each purification if the same protein is going to bepurified; it is sufficient to strip and recharge it after 5–7purifications, depending on the cell extract, extract volume,target protein, etc.Recommended stripping buffer: 20 mM sodium phosphate,0.5 M NaCl, 50 mM EDTA, pH 7.4Strip the column by washing with at least 5–10 column volumes of stripping buffer. Wash with at least 5–10 column volumes ofbinding buffer and 5–10 column volumes of distilled water before recharging the column.Recharge the water-washed column by loading 0.5 ml or 2.5 ml of0.1 M NiSO4 in distilled water on HisTrap HP 1 ml and 5 ml column,respectively. Salts of other metals, chlorides, or sulfates, may also be used (see“Optimization”). Wash with 5 column volumes distilled water, and 5 column volumes binding buffer (to adjust pH) before storage in 20% ethanol.6Cleaning-in-placeWhen an increase in back-pressure is seen, the column can becleaned. Before cleaning, strip off Ni2+ ions using therecommended procedure described above.After cleaning, store in 20% ethanol (wash with 5 column volumes) or recharge with Ni2+ prior to storage in ethanol.The Ni2+-stripped column can be cleaned by the followingmethods;•Remove ionically bound proteins by washing the column with several column volumes of 1.5 M NaCl; then wash the columnwith approximately 10 column volumes of distilled water.•Remove precipitated proteins, hydrophobically bound proteins, and lipoproteins by washing the column with 1 MNaOH, contact time usually 1–2 hours (12 hours or more forendotoxin removal). Then wash the column withapproximately 10 column volumes of binding buffer, followedby 5–10 column volumes of distilled water.•Remove hydrophobically bound proteins, lipoproteins, and lipids by washing the column with 5–10 column volumes 30%isopropanol for about 15–20 minutes. Then wash the columnwith approximately 10 column volumes of distilled water.Alternatively, wash the column with 2 column volumes ofdetergent in a basic or acidic solution. Use, for example,0.1–0.5% nonionic detergent in 0.1 M acetic acid, contact time1–2 hours. After treatment, always remove residual detergentby washing with at least 5 column volumes of 70% ethanol.Then wash the column with approximately 10 column volumesof distilled water.7Scaling-upTwo or three HisTrap HP 1 ml or 5 ml columns can be connected in series for quick scale-up (note that back-pressure will increase).Ni Sepharose High Performance, the medium prepacked inHisTrap HP columns, is supplied preswollen in 25 and 100 ml labpacks (see Ordering Information). An alternative scale-up strategy is thus to pack the medium in empty columns – Tricorn™ and XK columns are suitable for this purpose.8StorageStore HisTrap HP columns in 20% ethanol at 4°C to 30°C.9TroubleshootingThe following tips may be of assistance. If you have any furtherquestions about your HisTrap HP column, please visit/hitrap, contact our technical support, or your local representative.Note:When using high concentrations of urea or Gua-HCl,protein unfolding generally takes place. Refolding on-column (or after elution) is protein-dependent.Tips:To minimize dilution of the sample, solid urea or Gua-HCl can be added.Tips:Samples containing urea can be analyzed directly by SDS-PAGE whereas samples containing Gua-HCl must be buffer-exchangedto a buffer with urea before SDS-PAGE.Column has clogged:•Cell debris in the sample may clog the column. Clean the column according to the section Cleaning-in-place.•It is important to centrifuge and/or filter the sample through a0.22 µm or a 0.45 µm filter, see Sample preparation. Sample is too viscous:•If the lysate is very viscous due to a high concentration of host nucleic acid, continue sonication until the viscosity is reduced,and/or add DNase I to 5 µg/ml, Mg2+ to 1 mM, and incubate onice for 10–15 min. Alternatively, draw the lysate through asyringe needle several times.Protein is difficult to dissolve or precipitates during purification:•The following additives may be used: 2% Triton X-100, 2% Tween 20, 2% NP-40, 2% cholate, 1% CHAPS, 1.5 M NaCl,50% glycerol, 20 mM ß-mercaptoethanol, 1–3 mM DTT or DTE(up to 5 mM is possible but depends on the sample and thesample volume), 5 mM TCEP, 10 mM reduced glutathione, 8 Murea, or 6 M Gua-HCl. Mix gently for 30 min to aid solubilizationof the tagged protein (inclusion bodies may require longermixing). Note that Triton X-100 and NP-40 (but not Tween)have a high absorbance at 280 nm. Furthermore, detergentscannot be easily removed by buffer exchange.No histidine-tagged protein in the purified fractions:•Elution conditions are too mild (histidine-tagged protein still bound: Elute with an increasing imidazole gradient ordecreasing pH to determine the optimal elution conditions.•Protein has precipitated in the column: For the nextexperiment, decrease amount of sample, or decrease proteinconcentration by eluting with linear imidazole gradient insteadof imidazole steps. Try detergents or changed NaClconcentration, or elute under denaturing (unfolding)conditions (add 4–8 M urea or 4–6 M Gua-HCl).•Nonspecific hydrophobic or other interaction: Add a nonionic detergent to the elution buffer (e.g. 0.2% Triton X-100)or increase the NaCl concentration.•Concentration of imidazole in the sample and/or binding buffer is too high: The protein is found in the flow-throughmaterial. Decrease the imidazole concentration.•Histidine-tag may be insufficiently exposed: The protein is found in the flowthrough material; perform purification ofunfolded protein in urea or Gua-HCl as for inclusion bodies.•Buffer/sample composition is incorrect: The protein is found in the flowthrough material. Check pH and composition ofsample and binding buffer. Ensure that chelating or strongreducing agents are not present in the sample at too highconcentration, and that the concentration of imidazole is nottoo high.SDS-PAGE of samples collected during the preparation of thebacterial lysate may indicate that most of histidine-tagged protein is located in the centrifugation pellet. Possible causes andsolutions are:•Sonication may be insufficient: Cell disruption may be checked by microscopic examination or monitored bymeasuring the release of nucleic acids at A260. Addition oflysozyme (up to 0.1 volume of a 10 mg/ml lysozyme solution in25 mM Tris-HCl, pH 8.0) prior to sonication may improveresults. Avoid frothing and overheating as this may denaturethe target protein. Over-sonication can also lead tocopurification of host proteins with the target protein.•The protein may be insoluble (inclusion bodies): The protein can usually be solubilized (and unfolded) from inclusion bodiesusing common denaturants such as 4–6 M Gua-HCl, 4–8 Murea, or strong detergents. Prepare buffers containing 20 mMsodium phosphate, 8 M urea, or 6 M Gua-HCl, and suitableimidazole concentrations, pH 7.4–7.6. Buffers with urea shouldalso include 500 mM NaCl. Use these buffers for samplepreparation, as binding buffer and as elution buffer. Forsample preparation and binding buffer, use 10–20 mMimidazole or the concentration selected during optimizationtrials (including urea or Gua-HCl).The protein is collected but is not pure (multiple bands on SDS polyacrylamide gel):•Partial degradation of tagged protein by proteases: Add protease inhibitors (use EDTA with caution, see Table2).•Contaminants have high affinity for nickel ions: Elute with a stepwise or linear imidazole gradient to determine optimalimidazole concentrations to use for binding and for wash; addimidazole to the sample in the same concentration as thebinding buffer. Wash before elution with binding buffercontaining as high concentration of imidazole as possible,without causing elution of the tagged protein. A shallowimidazole gradient (20 column volumes or more), mayseparate proteins with similar binding strengths. If optimizedconditions do not remove contaminants, further purificationby ion exchange chromotography (HiTrap Q HP orHiTrap SP HP) and/or gel filtration (Superdex™ Peptide,Superdex 75 or Superdex 200) may be necessary.•Contaminants are associated with tagged proteins: Add detergent and/or reducing agents before sonicating cells.Increase detergent levels (e.g. up to 2% Triton X-100 or2% Tween 20), or add glycerol (up to 50%) to the wash bufferto disrupt nonspecific interactions.Histidine-tagged protein is eluted during sample loading/wash:•Buffer/sample composition is incorrect: Check pH and composition of sample and binding buffer. Ensure thatchelating or strong reducing agents are not present in thesample at a too high concentration, and that theconcentration of imidazole is not too high.•Histidine-tag is partially obstructed: Purify under denaturing conditions (use 4–8 M urea or 4–6 M Gua-HCl).•Column capacity is exceeded: Join two or three HisTrap HP1 ml columns together or change to a HisTrap HP 5 ml column. 10Intended useThe HisTrap HP is intended for research use only, and shall not be used in any clinical or in vitro procedures for diagnostic purposes.11Ordering InformationProduct No. supplied Code No.HisTrap HP 5 × 1 ml 17-5247-01100 × 1 ml1 17-5247-051 × 5 ml 17-5248-015 × 5 ml 17-5248-02100 × 5 ml1 17-5248-05 Related products No. supplied Code No.100 ml 17-5268-02 HiTrap Desalting 5 × 5 ml 17-1408-01100 × 5 ml1 11-0003-29 PD-10 Desalting Column 30 17-0851-01 HiPrep 26/10 Desalting 1 × 53 ml 17-5087-014 × 53 ml 17-5087-02HisTrap FF 5 × 1 ml 17-5319-01100 × 1 ml1 17-5319-025 × 5 ml 17-5255-01100 × 5 ml1 17-5255-02 HisTrap FF crude 5 × 1 ml 11-0004-58100 × 1 ml1 11-0004-595 × 5 ml 17-5286-01100 × 5 ml1 17-5286-02 HisTrap FF crude Kit 1 kit 28-4014-77 HisPrep™ FF 16/10 1 × 20 ml 28-9365-511Pack size available by special order.1 One connector included in each HiTrap package.2 Two, five, or seven stop plugs female included in HiTrap packages depending on the product.3One fingertight stop plug is connected to the top of each HiTrap column at delivery.AccessoriesNo. Supplied Code No.1Tubing connector flangeless/M6 female 12 18-1003-68Tubing connector flangeless/M6 male 1 2 18-1017-98Union 1/16” female/M6 male 1 6 18-1112-57Union M6 female /1/16” male 1 5 18-3858-01Union luerlock female/M6 female 218-1027-12HiTrap/HiPrep, 1/16” male connector for ÄKTA design8 28-4010-81Stop plug female, 1/16”2 5 11-0004-64Fingertight stop plug, 1/16”35 11-0003-55Related literatureCode No.Recombinant Protein Purification Handbook, Principles and Methods18-1142-75Affinity Chromatography Handbook, Principles and Methods18-1022-29Affinity Chromatography, Columns and Media Selection Guide18-1121-86Ni Sepharose and IMAC Sepharose, Selection Guide 28-4070-92HiTrap Column Guide18-1129-81。
ProductCatalogRF Power Solutions forWireless InfrastructureNovember 2023The Leading GlobalPartner in RF PowerCreated in 2015, Ampleon is shaped by 50 years of RF Power leadership and is set toexploit the full potential of data and energy transfer in RF. We share the passion for RFtechnology which is what we radiate to our customers, suppliers and partners.Since 2019, 5G NR (New Radio) is rolling out and it translates into new, extremelychallenging requirements for our RF Power components. Ampleon is addressing theserequirements with technology-agnostic solutions, utilizing market-leading LDMOS, GaNas well as other semiconductor technologies.The continuous increase in cost and environmental awareness is forcing the basestation efficiency requirements to reach new levels. At the same time, we see a trendtowards higher power and higher bandwidth product solutions. These developmentsspur Ampleon’s highly talented engineers to develop new architectures and designapproaches which enable more compact and less visible base stations.As the demand for wireless infrastructure services grows rapidly, operators are facedwith the need to get much more capacity from their dedicated frequency spectrum. Thischallenge can be addressed with Multiple Input Multiple Output (MIMO) technology.Conventional MIMO typically uses two transmit and two receive antenna elements todouble the capacity. Massive MIMO (mMIMO), however, goes further and is using up to64 simultaneous transmit and receive streams to create a much higher network capacity.Ampleon is offering integrated RF power solutions for 5G mMIMO base stations as well asfor small cell and macro base stations.Download the latest version/mpc2Wireless Infrastructure Product Catalog - November 2023 | Wireless Infrastructure Product Catalog - November 2023 | 3Wireless Infrastructure Product Catalog - November 2023 | 4Recommended PA SolutionsLine-up Peak Power800 W500 W300 W48 V LDMOSBLM9H0610S-60PGBLP9H10S-850AVT70 W28 V LDMOSBLP9G0722-20GBLC10G15XS-301AVT BLM9D1822-30B3 - 8 W 1.8 - 3.8 GHz xiD28 V LDMOSB11G3338N81D 28 V LDMOSB11G1822N60D BLC10G19XS-600AVT 40 WFrequency10 W1 GHz1.8 GHz2.7 GHz3.6 GHz 5 GHz 48 V LDMOSBLP9H10-30GBLC9H10XS-505AB10G2327N55D BLM9D0708-05AM BLM9D0910-05AMWireless Infrastructure Product Catalog - November 2023 | 5Macro ProductsThe RF Power transistor selection guide is available on: /products/mobile-broadband Its easy-to-use-parametric filters help you choose the right RF power transistor for your design.When selecting Ampleon’s Macro solutions you choose:• A full line-up of solutions for which Driver and Finals work seamlessly together, covering 4G and 5G requirements as well asmobile legacies• A combination of best-in-class, reliable and secure LDMOS technology, together with low-cost and outstanding thermal packaging and advanced design methodologies, all of which are produced and tested with highly automated volume-scale capabilities, delivering: - Very consistent and reliable performance - High line-up gain with low gain variation - High linearized efficiency- Record power and efficiency from a single packaged transistor across different frequency bands- Compact and cost-effective line-up solutions, thanks to integrated drivers and Doherty optimized finalsMacro FinalsMacro Drivers6Wireless Infrastructure Product Catalog - November 2023 | Wireless Infrastructure Product Catalog - November 2023 | 7Wireless Infrastructure Product Catalog - November 2023 | 8Massive MIMO ProductsThe RF Power transistor selection guide is available on: /products/mobile-broadbandIts easy-to-use-parametric filters help you choose the right RF power transistor for your design.When selecting Ampleon’s massive MIMO (mMIMO) solutions you choose:• Ampleon’s Massive MIMO portfolio based on LDMOS and GaN integrated Doherty solutions, offers high consistentperformance in a compact size. Enabling cost efficiency and ease of use in 4G and 5G mMIMO PA’s: - Excellent DPD linearization with Ampleon’s LDMOS and GaN technology - Compact footprint to meet space requirements in mMIMO antennas - High line-up gain- Very consistent performance- Proven track record in high volume supplymMIMO Line-upmMIMO FinalsWireless Infrastructure Product Catalog - November 2023 | 9mMIMO DriversWireless Infrastructure Product Catalog - November 2023 | 10Small Cell ProductsThe RF Power transistor selection guide is available on: /products/mobile-broadbandIts easy-to-use-parametric filters help you choose the right RF power transistor for your design.When selecting Ampleon’s Small Cell solutions you choose:• LDMOS technology breakthrough within the GaAs dominated small cell market, offering:- Up to 300 MHz instantaneous bandwidth - Higher output power for coverage increase - Higher linearizable efficiency - Excellent DPD linearization- Very compact product family in standardized package footprint for ease of deploymentSmall CellACP3-1230-4SOT1250-4(32.2 x 10.1 x max 4.5 (mm))ACP3-1230-6SOT1258-5(32.2 x 10.1 x max 4.5 (mm))ACP3-780-4SOT1273-1(20.6 x 9.8 x max 3.7 (mm))* Not drawn to scalePackage PortfolioACP3-1230-6SOT1258-4(32.2 x 10.1 x max 4.5 (mm))Ampleon `s package overview is available on /packagesACP3-780-6SOT1275-1(20.6 x 9.8 x max 4.0 (mm))Overmolded Plastic (OMP) Packages*OMP-780-6FOMP-780-6F-1(20.57 x 9.78 x max 4.0 (mm))OMP-780-16GOMP-780-16G-1(20.75 x 9.96 x max 4.0 (mm))TO-270-2GSOT1483-1(10.67 x 6.1 x max 2.0 (mm))LGA 7x7LGA-7x7-20-1(7.0 x 7.0 x max 1.0 (mm))OMP-400-8GOMP-400-8G-1(10.3 x 10.3 x max 4.0 (mm))LGA 7x7LGA-7x7-20-2(7.0 x 7.0 x max. 1.0 (mm))OMP-780-4FOMP-780-4F-1(20.57 x 9.96 x max 4.0 (mm))OMP-1230-6FOMP-1230-6F-1(32.25 x 9.78 x max 4.0 (mm))PQFN 8x8SOT1462-1(8.0 x 8.0 x max 2.2 (mm))PQFN 12x7PQFN-12x7-36-1(12.0 x 7.0 x max 2.2 (mm))DFNDFN-4.5x4-6-1(4.0 x 4.5 x max. 0.85 (mm))DFNDFN-7x6.5-6-1(7.0 x 6.5 x max. 0.85 (mm))Air-Cavity Ceramic (ACP) Packages*SOT1249BSOT1249B(20.3 x 9.8 x max 4.65 (mm))Air-Cavity Plastic (ACP) Packages*Package namePackage version (L x W x H (mm))L e n gt h W thH gh tLGA 12x8LGA-12x8-34-2(12.0 x 8.0 x max. 0.98 (mm))Committed to Your SuccessAt Ampleon, we are passionate about your success. Rest assured that we deliver world class innovation fora broad range of applications. In line with your challenges increasing, we continuously improve and enhance our LDMOS technology and strengthen our footprint in GaN.During the entire process from design to delivery, you will enjoy outstanding technical support from well trained staff and knowledgeable Field Application Engineers (FAEs) as part of our distribution network. Whether you require load-pull data, application boards, samples, ADS / AWR models or other, you will be accompanied in every step on the way to success.Our application engineering resources are spread around the globe, with our offices (Nijmegen / The Netherlands, Toulouse / France, Smithfield / USA, Shanghai / China) providing local customer support.SupportDatasheets, test reports and simulation models are available online on: /support/documentation.To make sure your request is processed quickly and directed to the right contact partner at Ampleon, please contact us via:/contact.Order samplesTo support customers in designing new products, Ampleon supplies samples and demonstration boards.Samples can be requested via our online e-samples store: /samples (please register at first log-in).For inquiries, please contact your local sales representative listed on: /contact.Additional information• /products• /applicationsDevice Naming ConventionOperation frequency, for single band = highest frequency (22 = 2200 MHz), for multi-band (1822 = 1800 to 2200 MHz)F: Ceramic packageC: Air-cavity plasic (ACP) package M: MMICP: Overmolded plastic (OMP) package B: Semiconductor die made of Si C: Semiconductor die made of GaNG: 28-32 V supply voltage D: Integrated Doherty (28 V)AD: Advanced integrated Doherty (28 V)H:50 V supply voltageTechnology generationP 1dB power level @ the supply voltage of Datasheet; PAD and GaN = P 3dB V: Leads for external decoupling W: Supply through decoupling leads Gullwing shaped leadsGF LSA GVTItalic = OptionalBLC 10A: Asymmetric Doherty (PAD); asymmetric integrated Doherty P: Symmetric Doherty - push-pull configurationM: 50 ohm matched output T: Internal video decoupling M: Multi-chip deviceL: High-frequency power transistor - - PQFN / LGA / TO270LS ACC / ACP2S OMP780 / OMP400XS ACP3COMCPackage Naming ConventionOMP -ACC: Air-Cavity Ceramic Package ACP: Air-Cavity Plastic Package DFN: Dual No-lead Package H-PAM: High Power PAMLGA: Land-Grid Array Package MCM: Multi-Chip ModuleOMP: Overmold Plastic PackageP(QFN): (Power) Quad Flat No-lead Package PAM: Power Amplifier ModuleWCP:Wafer level Chip-scale Package12301230: SOT539780: SOT502650: SOT1228400: 10 x 10 mmL x B in mm for DFN / PQFN / MCM / PAM / FEM-FNone: No Leads (DFN / PQFN / MCM / PAM)F: Straight Lead (standard)G: Gull-Wing Lead (standard)S: Straight Wide Lead W: Gull-Wing Wide Lead-Outline versoin number08Total I/O count, excluding GND / heatsink / exposed die pad, including voltages1Notes。
第53卷第3期力学学报Vol.53, No. 3 2021 年 3 月Chinese Journal of Theoretical and Applied Mechanics Mar.,2021冰工程中的关键力学问题冰激振动中的锁频共振分析*1>黄国君2)(中国科学院流固耦合系统力学重点实验室，中国科学院力学研宂所，北京100190)摘要冰激振动（ice-induced vibration,IIV)中的锁频共振严重威胁结构安全，恶化人员工作环境，然而对其机理的认识仍然不清.本文基于作者和合作者以前建立的一个冰间歇破坏型IIV模型（黄国君和刘鹏飞，2009)对柔性结构的锁频共振机理进行了理论研究.应用该模型预报了发生在一个冰速区间内的锁频共振现象，并研宄了结构和冰特性参数：结构阻尼和刚度以及冰的压缩刚度和冰破坏的破坏区长度、軔脆转换速度和随机性对I1V及锁频共振的影响，在此基础上探索了锁频共振机理.研究表明：在锁频共振冰速区间内，结构响应和冰力主频都锁定在结构固有频率，然而不同冰速下的频谱结构和振动形态各异，从常规单频共振到多频共振、从等幅振动到振幅周期性变化的拍振动，呈现出丰富的动力学特征；结构和冰特性参数可改变锁频共振冰速区间的长度和位置以及结构振幅，冰破坏的随机性和应变率效应发挥着一种竞争作用；锁频共振来源于冰破坏的应变率效应，其力学机制是频率调制和对结构-冰动能传递的非对称性正反馈效应放大的双重作用，本文分析揭示的这一新的锁频共振机理属于耦合振动，与传统的负阻尼自激振动机制有着本质区别.本文分析结果及对锁频共振机理的认识有助于相关实验研究和冰区结构设计以及I1V减振技术的研发.关键词冰激振动，锁频，共振，冰的破碎强度，应变率效应中图分类号:U260.17 文献标识码：A doi: 10.6052/0459-1879-21-087STUDY ON FREQUENCY LOCK-IN RESONANCE IN ICE-INDUCED VIBRATION 11Huang Guojun2*{Institute o f M echanics, Key Laboratory fo r Mechanics in Fluid Solid Coupling Systems, Chinese Academy o f Sciences, Beijing100190, China)Abstract Frequency lock-in resonance in ice-induced vibration(IIV)threatens severely the safety of the structures and worsens the working environment for operators.Its underlying mechanism is unclear yet.This paper presents a theoretical study on the mechanism of the frequency lock-in resonance for compliant structures.The study is based on an intermittent ice-crushing type of IIV model developed previously by the author and co-worker(Huang and Liu,2009). The frequency lock-in resonance is predicted over an ice velocity span.Then the parametric analysis is performed on IIV and frequency lock-in resonance for some influential factors,including structural damping and stiffness,ice stiffness,ice-crushing zone length,ductile-brittle transitional ice-velocity and randomness in the ice-crushing strength and ice-crushing zone length. From these theoretical studies,the mechanism of the frequency lock-in resonance is investigated.It is shown that although both the predominant ice and structural response frequencies are locked to the structural natural frequency when frequency lock-in resonance takes place,the time history profiles of ice force and structural response and their frequency spectra2020~03-03 收稿,2021-03-16录用，2021-03-16 网络版发表.1) 国家自然科学基金资助项目（10772184).2)黄国君，副研究员，主要研究方向：结构动力学和材料力学.E-mail: ***************.cn引用格式：黄国君.冰激振动中的锁频共振分析.力学学报，2021，53(3): 693-702Huang Guojun. Study on frequency lock-in resonance in ice-induced vibration. Chinese Journal o f Theoretical and Applied Mechanics,__________2021,53(3): 693-702___________________________________________________________________________________________________________are different corresponding to the different ice velocity.Not only the conventional mono-frequency resonance with the uniform amplitude but also the multi-frequency beat resonance with the periodically changing amplitudes are predicated. For the frequency lock-in resonance,structural and ice properties affect the length and location of the ice velocity span as well as the response amplitude,and the randomness and strain rate effect in ice-crushing are the two competing factors. It is unveiled that the strain rate effect of the ice-crushing strength is responsible for the frequency lock-in resonance,by frequency modulation and by promoting the uneven kinetic energy transfer between ice and structures,a positive feedback mechanism.The present novel mechanism is a coupled vibration that is essentially different from the conventional one, i.e.,the negative damping in self vibration predicted from the continuous ice-crushing type of IIV models.The present result is instructive to the further systematic experimental study on the frequency loc-in resonance and to devising some effective techniques for the mitigation of intensive IIV.Key words ice-induced vibration,frequency lock-in,resonance,ice-crushing strength,strain rate effect694 力学学报2021年第53卷引言冰激振动（ice-induced vibration,IIV)中的锁频共振现象是指流动的浮冰与冰区结构（或冰盖与在其 中航行的交通船只如破冰船）的交互作用中，在一定 的冰速范围内冰力和结构振动的主频皆锁定在结构 固有频率，从而导致结构共振.其结构振幅可较常规 振幅有数量级的差异，这与祸激振动（vortex-induced vibration,VIV>中的锁频共振在动力学上是相似的HI,然而两者的物理本质完全不同.冰激锁频共振严重威 胁冰区结构的安全，导致结构疲劳加剧，甚至直接摧 毁结构，此外还会恶化结构上的人员工作环境和设 备运行条件.因此探索冰激锁频共振的力学机理、明确其产生的临界条件不仅具有重要的科学意义，而 且可以为冰区结构的设计和安全运行控制提供理论 指导，具有显著的工程价值.I IV己受到冰区相关国家学术界和产业界的广 泛关注P1，其中锁频共振是研究的重点和难点，为此 己开展了不少实验和理论研究.实验研宂包括现场监 测和实验室模型实验，较为代表的工作如:Engelbrek-tS〇n M在Bothnia海湾现场观察到冰激共振发生时，结构的加速度可达0.7g，大大超过人体可接受的振 动水平，而当天大多时间结构处于低幅振动水平，只有〇.〇7g左右，这表明冰激共振的出现具有一定的随 机性；Maattanenw通过实验室模型研究发现在一个 较宽的冰速范围内结构产生锁频共振;Tsuchiya等15】在实验室模型研究中发现结构的振动主频先随冰速 线性增加，然后锁定在结构固有频率直到最高实验 冰速，但冰力主频并未锁定在结构固有频率，离散性 较强，这也许与实验在空气中进行有关，这种锁频振动从严格意义上来说不属于锁频共振.另一方面，许多研宂者建立了 IIV动力学模型，以揭示IIV特别是锁频共振的动力学机制，并提供冰 区结构设计所需的动力学模型.根据冰破坏过程的 连续性，可将现有的IIV动力学模型分为两大类.一类是以Blenkam【61和MaattSnen [7丨最初建立并发展 起来的基于负阻尼机制的冰连续破坏型自激振动模 型，该类模型将IIV过程中冰的破坏视为连续压碎 过程，所以冰力就是冰的破坏冰力，可由冰的压缩强 度计算得到.基于PeytonW建立的冰的压缩强度与 冰速的相关性曲线，该曲线在一定的冰速区间内梯 度为负，为结构提供负阻尼，从而导致结构发生动力 学失稳，产生自激振动，结构响应主频以及相应的冰 力主频自然皆锁定在结构固有频率.自激振动模型 简单、操作方便，是目前应用最广泛的IIV动力学模 型[911].另一类模型认为IIV中冰的破坏过程是间歇 的，即冰的破坏存在一个特征长度，这等效于认为冰 存在破碎频率，它等于冰速除以该特征长度.基于该 认识Matlock1121最先建立了一个冰间歇破坏型I1V 动力学模型，可以反映在低速和高速冰速段内结构 响应较小、在中间冰速范围内结构响应较大的全冰 速范围IIV实验的一般特征，但不能预报1IV锁频共 振.Sodhi|13l (下称Sodhi模型）对Matlock模型进行 了改进，对冰与结构的交互作用考虑相互接触的加 载阶段同时，还考虑了冰板压碎、屈曲破坏以后结构 清除碎冰的过程以及冰与结构接触过程中可能存在 的分离过程，它包含了更多的物理过程细节，因而更 为合理.然而正如本文下面将要介绍的该模型虽然 能够预报I1V共振的出现，但不能预报在一定冰速范 围内的锁频共振.同样作为冰间歇破坏型IIV 动力学第3期黄国君：冰激振动中的锁频共振分析695模型,Toyama等【14】和Shih_针对共振发生时结构 响应与冰力的同相位特征，提出了一些结构运动学 假设，以建立各自的IIV模型，探索冰激共振产生的 临界条件和结构响应幅值.这些冰间歇破坏型1IV模 型不是一个全冰速范围内的一般性动力学模型，其 中的运动学假设只适用于研究共振产生时的必要条 件，不能研宄复杂的锁频共振现象.Huang等【|6]在 Sodhi模型的基础上，通过引入Peyton[8】建立的冰 的压缩强度与冰速相关性的动力学特性，建立了一 个全冰速范围冰间歇破坏型IIV动力学模型（下称 Huang-L iu模型)，该模型吸收了两类模型的优点，不 仅可以预报低速和高速冰速区段的小振幅IIV，而且 可以预报中间冰速范围内可能发生的锁频共振，这 是首个能预报锁频共振的间歇破坏型I1V动力学模 型.目前Huang-L iu模型己受到学术界关注[9.17_27]，Jeong和Baddour117]对该模型和Toyama模型[|4]进 行了理论对比;Hendrikse等基于该模型发展了IIV模型分析风电等柔性结构的IIV和疲劳寿命；最 近Abrasion等[271也用该模型计算结果评估它们新建 的基于非线性动力学的IIV模型.此外也有学者提出 了唯象学IIV模型，徐继祖和王翎羽基于1IV与 V IV的动力学相似，引入一个冰力振子方程，与振动 方程联立建立了他们的IIV模型，可以反映IIV锁频 共振现象;X u和Oterkus等[21】对该模型进行了改进,计及了冰压缩强度与冰速的相关性，但该类模型未 涉及冰与结构交互作用的物理过程，无法揭示IIV及 其锁频共振的物理机制.对IIV锁频共振的研宄已有50多年的历史，但 目前对于其机理的认识仍然不清，是自激振动还是 强迫振动存在较大争议，达到Maattanenn9]所期望的 共识尚需开展更深入的实验和理论研宄工作.本文 应用Huang-Liu模型开展冰激锁频共振的理论研究，首先分析IIV及锁频共振的结构响应特征，并从结 构响应和冰力的频率耦合特性以及Huang-Liu模型 与Sohdi模型计算结果的对比来研究锁频共振产生 的原因；然后再分析结构特性和冰的物理特性参数 对锁频共振影响的一般趋势；最后在此基础上揭示 锁频共振的动力学机制.1IIV动力学模型1161考虑一个单自由度振子结构系统与运动冰板的交互作用，冰的破坏为间歇式，假设存在…个破坏区 特征长度，作用过程可分为3个阶段:加载，(碎冰)挤 出和可能的分离阶段[|31.系统的运动控制方程为Mx+C x+K x^k[x〇 +vt-x -p(n- 1)]+ F e,0 < < 5f(loading phase)F e，Sf<6<p and x^v-(1)(extrusion phase)0，S<0or(6f^S<p and i> v)(separation phase)式中，M,C和K分别为结构质量、阻尼系数和刚 度；X, X和X分别为结构位移、速度和加速度，为;c的初值八为完整冰（破坏前）的压缩刚度；<5 = _*：〇+ V f- - /?(«- 1)为结构压入冰的长度，其中V，和 «分别为冰速、冰间歇破坏的破碎区长度和破碎区序 号;<5f = (Ff- Fe)/A:为冰破碎时的压入长度，其中Fe 为挤出阶段挤出碎冰的冰力，设为常数，F f为冰破碎 时的瞬时破坏冰力.式（1)对Huang-L iu模型|16]的运动控制方程稍作了改进，在加载阶段条件中去掉 了太< V，并在分离阶段条件中增加了 <5 < 0,其表述 更为确切.根据Korzhavin[3G]，破坏冰力为Ff=ImxhDcrf(2)式中，/，W和〃分别为压入、几何和接触系数；为 结构的直径；A为冰的厚度;£T f为冰的压碎强度.在 Sodhi模型中，冰的破坏冰力取为常数，亦即压碎强 度取为常数；而在Huang-L iu模型中〇•(■依赖于冰相 对于结构的速度= v-力，该相关性就是PeytonW建 立的冰的压碎强度与冰速的相关性曲线，如图1所 示，图中定义了相关特征参数，其中应变率备=V t//!，vt为軔脆转换冰速.根据Iliescu和Schulson13"的研 宄，该曲线可以表示为无量纲形式，由两个幂分布表 示为(1-o'f d K V r/V t f+^f d,Vr/V t < 1 ⑶(1 -7fb)(vr/vt户+ Jfb，V r/v t〉1式中，= ^"f/C fm ax，afd = ffd/C fm ax，Cfb =这里ffmax为相应于A或V t的最大冰破碎强度，a> 0 和0<0为对应的无量纲指数.696力学学报2021年第53卷构响应高度依赖于结构与冰的相对运动.因此式（5)整体上是高度非线性的，其求解需要与式(3)和式(6)联立获得.在数值求解过程中的每个时间步长，都需要根据式(5)中给出的各阶段条件，判断当前结构所处的阶段，从而由相应的封闭解析解获得结构响应和冰力的全部时间历程.2锁频共振图1冰压碎强度与应变率关系的特征图Fig. 1Characteristic plot of ice-crushing strength versus strain rate 引入下面无量纲参数和变量x=x/A, x〇 =x〇/A, p=pi A, 6=6/A6f = 8flA, t = a>n t, k = k/K—^e/^f m a x i V—v/ (〇Jn^) ,Vt — Vt/(〇J n/I)(4)式中，zl = Ffm ax/A■为相应于最大破坏冰力的最大结 构静态位移;w n= V^/而为结构的固有圆频率，这样 控制方程式（1)可转化为无量纲形式应用Huang-L iu模型可对IIV进行数值分析，重 点关注所预报的锁频共振.表1列出了式(3)、式(5)所涉及的表征冰和结构性质的无量纲参数，以此作 为一个代表算例，通过计算获得相应的结构响应和 冰力时间历程.表1冰和结构特性参数Table 1Typical parameters of the properties ofice and structuresk孑fd^"fb a P P0.10.040.70.50.5-21100.2x + 2^x-h x=k[x〇-h v t-x-p(n- 1)] +F e»0<5<(loading phase)F e,6f<：S<p and x4：v{.⑶(extrusion phase)0，6<0or6f^6<p and x>v(separation phase)其中，f = C V(2Mwn)为结构阻尼比，= d2je/(dr2)，无=dS/dr.由式（2)可得/V =內，因而瞬时破坏压 入长度为&(vr/v t)=<5-f(vr/v t) -F e(6)式（5)为分段线性的非线性方程组，相当于间歇非 线性.在各阶段求解线性方程可获得各阶段的封闭解析解，其详细解可参考H uang和Liu的研 究（更正该文献中的两个打印错误：（1)式（10)下的变量解释中t= [/I+ i应为卜=0(1 + 幻；（2)式（11)中的应为[知+扮0e-戶e)]sin叫r e).应该指出的是由于冰破坏 强度的率相关性，式(6)所示的破坏压入长度与结构 瞬时速度相关，因此式（5)各阶段所经历的时间实际 上是结构运动相关的，这导致冰力的时间历程和结在运动冰的作用下结构从瞬态振动逐步过渡到 稳态振动，它对应稳定吸引子的极限环.图2黑线表 示结构稳态振动阶段的无量纲振幅J fm a x- 4in随无 量纲冰速v/vt变化的情况，可以看到在低冰速和高 冰速段结构振动较平和，而在中间段冰速段结构振 动较剧烈，这一 IIV总的趋势与实验发现的一般特征 是一致的.特别应该注意的是在v/vt = 2.2〜2.75的冰速区间，结构振动最为剧烈,较高冰速段的振动幅 值高10倍左右.图2中红线表示的是基于Sodhi模 型的计算结果，该模型计算中破坏冰力无速度相关 性，取为常数0.78Ffm ax.可以看到：虽然两个模型预 报的I1V总趋势一致，甚至在低冰速和高冰速段预报 结果几乎相同，但在中间冰速段，Huang-Liu模型预 报的IIV更为剧烈，这清楚显示出既使在冰间歇破坏 的情况下，冰破坏强度的率相关性在I1V中仍具有重 要的作用.为了揭7T C冰破坏率相关效应放大振动的原因，对上述Huang-Liu模型计算得到的稳定阶段结构位 移和冰力时间历程进行了频谱分析，分别获得了响 应主频/s和冰力主频/；，用结构固有频率/…进行 无量纲化，它们随相对冰速的变化表示在图3中，其中蓝色实线和虚线表示响应主频，红色方块表示 冰力主频.响应主频先随时间线性增加，在无量纲冰第3期黄国君：冰激振动中的锁频共振分析697图2不同模型预报的结构位移响应随冰速的变化Fig. 2 Dependence of the amplitude of structural deflection on the icevelocity predicted from the different models respectively图3图2计算结果对应的冰力和结构响应主频随冰速的变化 Fig. 3 Dependence of the predominant frequencies of the ice force andstructural response on ice velocity, corresponding to Fig.2速v /vt = 2.2时出现稳定解的分叉，原蓝色斜线代 表的吸引子失去稳定性，其主频由实线改为虚线表 示；在v /vt =2.2〜2.75区间新生长出一个稳定的吸 引子，其主频锁定在结构固有频率，用蓝色水平实线 表示，这一计算结果与Tsuchiya 等W 的实验结果相 同，不过实验中的最高实验冰速未超过平台段；有 趣的是在v /vt = 2.6〜2.75区间，原蓝色斜线代表的 吸引子又恢复稳定，因而蓝色虚线又改为实线表示， 这意味着在该区间出现了两个稳定吸引子，代表两 种稳态振动状态，系统选择哪种状态具有初值敏感 性，它与结构初始位置和速度相关[16];当无量纲冰 速v /vt > 2.75时，主频锁定的吸引子失去稳定性，锁 频平台消失，系统又经历一次分叉回到蓝色实线表 示的单个吸引子状态，平台前后的蓝色实线和平台 中的蓝色虚线几乎是一条斜线.同时可以观察到，除 了部分冰速区段以外冰力主频与响应主频几乎相同，特别是在v /vt = 2.2〜2.75区段，冰力主频和响应主 频皆锁定在结构固有频率，即结构发生了锁频共振, 所以可称上述锁频平台对应的振动状态为共振吸引 子，这正是该冰速段结构振动剧烈的原因.另外注意 到无量纲冰速v /vt 在0.75附近和1.0〜1.75区段，发 生了冰力主频锁定在结构固有频率的现象，但与响 应主频分离，该种锁频开始产生时对应的响应主频 分别在/…/4和/…/2附近,即分数频响应，所以结构响 应有一定放大，但没有锁频共振显著，可称该种锁频 为分离锁频，以与共振锁频相区别.冰力的分离锁频尚未见实验报道，可能是冰破坏的随机性妨碍了该 种锁频的产生.图3中黑色虚线给出了冰的无量纲特征破碎频率随相对冰速的变化，它被认为是冰的固有特性，与结 构运动无关，相当于冰与刚性结构作用的破碎频率. 同时对Sodhi 模型的计算结果进行了频谱分析，结果 表明响应主频和冰力主频相同，并沿图3中蓝色实 线和虚线连续变化，无一定冰速区内的锁频共振发 生.黑色虚线变成蓝线表明：对于柔性结构，冰力主 频及响应主频是结构与冰的相对运动和冰间隙破坏 复杂耦合的结果，冰破坏的率相关性进一步增强了 这种耦合，导致锁频发生.3锁频共振的影响因素分析为进一步了解锁频共振的特点，下面分析结构动力学参数和冰的力学及破坏特性参数对锁频共振影响的一般趋势，为抑制和控制剧烈的IIV 提供理论 指导.从控制方程式(5)和冰破坏的率相关性方程式(3)出发，选择的影响因素包括结构阻尼比f 和刚度 心冰的压缩刚度t 破坏区长度P 和初脆转换速度 i另外，考虑到脆性材料的破坏具有一定的离散性， 将研宄冰的破碎强度和破坏区长度一定的随机性对 锁频共振的影响.计算基本参数采用表1所列参数， 分别改变其中的参数，将计算结果与图2结果比较， 进行锁频共振的参数分析.图4(a )表示结构阻尼比对IIV 及锁频共振的影 响，其中黑线代表图2中的计算结果.当其他参数不 变仅改变f 的大小，可以看到增加结构阻尼使锁频 共振冰速区间段缩小，振动幅值减小，直至锁频共振.2.0.8.6.4.2.0.8.6.4.2<o y - n11 1* 11 n o 〈m ymFig. 4 Influence of the structural properties on the frequencylock-in resonance6 _—k/K=0.\消失.图4 (b >表示结构刚度对1IV 及锁频共振的影 响，改变刚度后最大结构静态位移」和结构固有频 率将改变，因而表1所列的相关无量纲参数也要相应改变.为比较方便，结构位移仍以图2算例的最大 静态位移扣无量纲化，它对应结构刚度可看到 随着结构刚度的提高，锁频共振冰速区间逐渐向高 冰速段移动，共振振幅也逐渐变小，直至锁频共振消 失，所以锁频共振容易在柔性结构中发生.图5(a )表不冰的相对压缩刚度[=/c/A ■对1IV 及锁频共振的影响，随刚度[减小，共振锁频区向高冰速端移动，区间宽度增加，振动加剧.图5(b )表示 冰的破碎区长度对IIV 及锁频共振的影响，随破碎区 长度增大，锁频共振冰速区间逐渐向高冰速段移动， 共振振幅也逐渐增大，不过变化非单调，在破碎区长 度万=15时，锁频共振区间消失，振幅减小，所以锁 频共振发生的冰破碎区长度要小于一定长度.图5(c ) 表示冰的軔脆转换速度P t对IIV 及锁频共振的影响, 可看到其影响较为显著，随A 增加锁频共振区间向 高冰速端移动，振动幅值有显著增大.为考察冰破坏 的随机性对锁频共振的影响，分别对冰的压碎强度 内和破坏区长度万加入了 10%, 20%和30%的均匀分布随机涨落，这样控制方程式(5)实际上是非线性 随机微分方程组，计算结果如图5 (d )所示，可看到随 机性增加使锁频共振冰速区间宽度和振动幅值减小， 区间位置向低速段稍有移动，30%的涨落时锁频共振6--= 10(a )阻尼(a) Damping(b )刚度 (b) Stiffness图4结构性质对锁频共振的影响23v/v,(a )压缩刚度(a) Compresion stiffness23v/v,(b )破碎区长度 (b) Crushing zone length图5冰的性质对锁频共振的影响))报2021年第53卷v /(J —J )s i r —J)Fig. 5 Influence of the ice properties on thefrequency lock-in resonance第3期黄国君.•冰激振动中的锁频共振分析699J I ■ 0% randomness -10% randomnessW(〇jt A)v/v,(c)初脆转换速度（d)破坏的随机性(c) Ductile-brittle transitional velocity (d) Randomness in crushing图5冰的性质对锁频共振的影响（续）Fig. 5 Influence of the ice properties on the frequency lock-in resonance (continued)己消失，所以冰破坏的率相关性和随机性是一种竞 争关系，它们对锁频共振起着相反作用.冰破坏的随 机性增加了 IIV的复杂性，还会引起系统在共振吸引 子和常规小幅振动吸引子之间随机游走[161，这可解 释EngelbrektsonW的现场观测结果.由以上结构和冰参数的影响分析可以看到它们 对锁频共振的影响较为复杂，对这些参数影响机理 的理解还有赖于对锁频共振力学机制的清晰认识.4锁频共振机理分析前面的分析表明了锁频共振来源于冰破坏的应 变率效应，下面将研究该效应作用的力学机制，分析 为什么共振能维持在一定冰速区间内发生.为此对 图2锁频共振冰速段中典型冰速的稳态结构速度响 应vs和冰力时程曲线进行分析，以了解冰与结构接 触过程和冰破坏过程对IIV及锁频共振的影响.图6(a)表不在v/vt= 2.2时稳态振动的结构速度 响应vs和冰力时程曲线，该冰速对应锁频共振区间 的开始冰速.加载阶段及其冰力呈周期变化并与响 应周期相同，一个响应周期发生一次冰的破坏，导致 冰力与响应完全同步，这就是常规的单频共振.冰力 历程中加载阶段冰力曲线与时间坐标所围面积就是 冰破坏前冰与结构之间所传递的动量，在该冰速整 个加载阶段内结构与冰运动方向都相同（vs > 0)，即冰力所做外力功全部转化为结构动能的增加，结构 不断从冰获取动能，直至一个周期内结构动能与结构黏性耗散能和势能达到平衡，结构稳定在高幅振 动状态.在v/vt = 2.2时Sodhi模型也能预报出完全 相同的共振，但其预报的共振只发生在这一冰速，不 存在锁频共振持续发生的冰速区间.图6(b)表7K v/vt = 2.6时稳态振动的结构速度响 应和冰力时程曲线，该冰速对应振幅最大冰速.在该 冰速下结构振幅出现了周期变化，也就是出现了拍 现象[32]，这是因为响应和冰力产生了多频，其主频都 接近结构固有频率，但围绕其附近还出现了两个对称 的次频，它们可以合成为频率为结构固有频率的拍振 动，其拍频为两个次频的差频，拍振动与主频振动叠 加就是图6(b)所示的振动.可以观察到在一个拍内 有10个振动周期并发生了 10次冰的间歇破坏.另外 在一个拍内加载过程逐渐从结构与冰运动方向相同 过渡到两者方向相反，同时结构振幅也从逐渐增大过 渡到逐渐减小，直至下一个拍开始.这是由于结构与 冰之间传递的动量使得结构逐渐从冰获得动能（当vs > 0)过渡到冰从结构获得动能（当vs < 0)，这说明 冰力既可激励振动也可抑制振动.v/vt = 2.6时的振 动可称为多频共振，其最大结构响应大于v/v, = 2.2 时的单频共振结构响应，但从平均来看其响应还是 小于单频共振时的响应.为了理解多频共振产生的原因，进一步分析 图6(b)所示v/V| = 2.6时稳态振动的结构速度响应和 冰力时程曲线.在一个拍内各加载时间长度和冰力幅 值（破坏冰力）也从逐渐增大过渡到逐渐减小，这意。
Optimum Technology Matching ® AppliedGaAs HBTInGaP HBTGaAs MESFET SiGe BiCMOS Si BiCMOSSiGe HBTGaAs pHEMTSi CMOS Si BJTGaN HEMT Functional Block DiagramRF MICRO DEVICES®, RFMD®, Optimum Technology Matching®, Enabling Wireless Connectivity™, PowerStar®, POLARIS™ TOTAL RADIO™ and UltimateBlue™ are trademarks of RFMD, LLC. BLUETOOTH is a trade-mark owned by Bluetooth SIG, Inc., U.S.A. and licensed for use by RFMD. All other trade names, trademarks and registered trademarks are the property of their respective owners. ©2006, RF Micro Devices, Inc.Product DescriptionOrdering InformationRF MEMSLDMOSGaAs HBT PRE-DRIVER AMPLIFIERThe RF3809 is a GaAs pre-driver power amplifier, specifically designed for wireless infrastructure applications. Using a highly reliable GaAs HBT fabrication process,this high-performance single-stage amplifier achieves high output power over a broad frequency range. The RF3809 also provides excellent efficiency and thermal stability through the use of a thermally-enhanced surface-mount plastic-slug pack-age. Ease of integration is accomplished through the incorporation of an optimized evaluation board design provided to achieve proper 50 Ω operation. Various evalua-tion boards are available to address a broad range of wireless infrastructure appli-cations: NMT 450 M Hz; GSM850 M Hz; GSM900 M Hz; DCS1800 M Hz;PCS1900 M Hz; and, UMTS2200 M Hz.FeaturesHigh Output Power of 2.0 W P1dB High LinearityHigh Power-Added Efficiency Thermally-Enhanced PackagingBroadband Platform Design Approach, 450 M Hz to 2500 M HzApplicationsGaAs Pre-Driver for Basestation AmplifiersPA Stage for Commercial Wire-less InfrastructureClass AB Operation for NMT, GSM, DCS, PCS, and UMTS Transceiver Applications2nd/3rd Stage LNA for WirelessInfrastructureRF3809GaAs HBT Pre-Driver AmplifierRF3809PCK-410Fully Assembled Evaluation Board, 450 M HzRF3809PCK-411Fully Assembled Evaluation Board, 869 M Hz to 894 M Hz RF3809PCK-412Fully Assembled Evaluation Board, 920 M Hz to 960 M Hz RF3809PCK-413Fully Assembled Evaluation Board, 1800 M Hz to 1880 M Hz RF3809PCK-414Fully Assembled Evaluation Board, 1930 M Hz to 1990 M Hz RF3809PCK-415Fully Assembled Evaluation Board, UMTS9Package Style: SOIC-8Absolute Maximum RatingsCaution! ESD sensitive device.Exceeding any one or a combination of the Absolute Maximum Rating conditions may cause permanent damage to the device. Extended application of Absolute Maximum Rating conditions to the device may reduce device reliability. Specified typical perfor-mance or functional operation of the device under Absolute Maximum Rating condi-tions is not implied.RoHS status based on EU D irective 2002/95/EC (at time of this document revision).The information in this publication is believed to be accurate and reliable. However, no responsibility is assumed by RF Micro Devices, Inc. ("RFMD") for its use, nor for any infringement of patents, or other rights of third parties, resulting from its use. No license is granted by implication or otherwise under any patent or patent rights of RFMD. RFMD reserves the right to change component circuitry, recommended appli-cation circuitry and specifications at any time without prior notice.Theory of Operation and Application InformationRF3809 design accommodates use in a variety of applications:•Linear driver from 450 M Hz to 2500 M Hz•2nd/3rd stage high linearity LNA, with noise figure in the 3 d B to 4 d B range from 800 M Hz to 2200 M Hz•High efficiency (> 50%) output stage for non-linear applicationsNominal data sheet shows specification for V CC=V BIAS=V REF=8V. RF3809 can easily be configured for 5 V operation, with a simple bias resistor change at V REF.. “Bias Table” on page 5 shows resistor values for V CC=V BIAS=V REF=5V. Generally speak-ing, 5 V data will compare to that for 8 V as follows:• 3 d B to 3.5 d B reduction in OP1dB•0.4 d B to 0.5 d B increase in small signal gainFor operation at other than 5 V, bias R can be calculated as follows (V CC=V BIAS=V REF=5V is used here to illustrate, operation at different voltage is determined with same methodology).e nominal 8 V case as a starting point: V CC=V BIAS=V REF=8V, I REF=15 m A, I CQ=258 m A. Target condition will be toachieve same I CQ with V CC=V BIAS=V REF=5V.ing evaluation board with separate lab supplies on (V CC/V BIAS) and (V REF), set V CC/V BIAS=5V, V REF=8V. I REF is main-tained at 15 m A, and I CQ drops from nominal value of 258 m A.3.V REF can then be increased > 8V until I CQ is restored. I REF increase to 23 m A is required (as seen in “Bias Table” on page 5).4.At this point, pin voltage at V REF is calculated (or measured with DVM): V PIN=V REF at eval board input – I REF*b ias R =10.8 –0.023 *300 =3.9 V.5.Next, calculate new bias R for V REF=5V: Bias R =(5 –3.9)/0.023 =47.8 Ω. See “Bias Table” on page 5, standard resistorvalue =47 Ω is called out. In this way, bias R can be calculated for any V CC=V BIAS=V REF configuration. The maximum I REF limit for RF3809 =30 m A.Junction-to-case thermal resistance (R TH_JC) is shown versus output power in the graph section of this data sheet. The graph was generated with nominal V CC=V BIAS=V REF=8V, I REF=15 m A, where ambient temperature =85 °C. Using this curve along with operating condition, junction temperature can be calculated. Resultant T J for this case yields MTTF ≥100 years. Standard RF3809 evaluation boards are matched for high efficiency at O P1dB. To ensure reliability for operation at high power, output match achieving equivalent or better efficiency on system board should be the goal.Typical s-parameter responses for each evaluation board are shown within the data sheet. These boards were matched with two specifications in mind:•Output load impedance set for optimum OIP3/ACP (Adjacent Channel Power for commonly used modulation standards).•Output load impedance set for high efficiency at O P1dB, with ruggedness (survival) into output 4:1 VSWR.In some cases, low power operation being one, it may be desirable to improve output return loss seen on evaluation board. This can be done with output match adjust. The result will be an increase in small signal gain. Tradeoffs between return loss, gain, OIP3, and compression point can then be considered in obtaining optimum performance for a particular application. Finally, infrastructure qualification report for RF3809 can be obtained by contacting RFMD.Package Drawing400 M Hz (RF3809410)Evaluation Board Schematic800 M Hz to 1000 M Hz (CDMA800, ISM, EGSM)869 M Hz to 894 M Hz (GSM800) (RF3809411)Evaluation Board Schematic920 M Hz to 960 M Hz (GSM900) (RF3809412)1805 M Hz to 1880 M Hz (DCS1800) (RF3809413)Evaluation Board Schematic1930 M Hz to 1990 M Hz (PCS1900) (RF3809414)UMTS (RF3809415)Evaluation Board Layout Board Size 2.0” x 2.0”PCB Design RequirementsPCB Surface FinishThe PCB surface finish used for RFMD's qualification process is electroless nickel, immersion gold. Typical thickness is 3 μinch to 8 μinch gold over 180 μinch nickel.PCB Land Pattern RecommendationPCB land patterns for PFMD components are based on IPC-7351 standards and RFMD empirical data. The pad pattern shown has been developed and tested for optimized assembly at RFMD. The PCB land pattern has been developed to accommodate lead and package tolerances. Since surface mount processes vary from company to company, careful process development is recommended.PCB Metal Land PatternPCB Solder Mask PatternLiquid Photo-Imageable (LPI) solder mask is recommended. The solder mask footprint will match what is shown for the PCB metal land pattern with a 2 m il to 3 m il expansion to accommodate solder mask registration clearance around all pads. The center-grounding pad shall also have a solder mask clearance. Expansion of the pads to create solder mask clearance can be provided in the master data or requested from the PCB fabrication supplier.Thermal Pad and Via DesignThe DUT must be connected to the PCB backside ground through a low inductance, low thermal resistance path. The required interface is achieved with the via pattern shown below for both low inductance as well as low thermal resistance. The footprint provided below worked well on the RFMD 20 m il thick Rogers 4350 PCB and also standard FR4. The vias are 8 m il vias that are partially plated through and are finished to 8 m ils ±2 m ils with a minimum plating of 1.5 m il. Failure to place these vias within the DUT mounting area on the PCB in this prescribed manner may result in electrical performance and/or reliability degrada-tion.Tape and Reel InformationCarrier tape basic dimensions are based on EIA 481. The pocket is designed to hold the part for shipping and loading onto SMT manufacturing equipment, while protecting the boyd and the solder terminals from damaging stresses. The individual pocket design can vary from vendor to vendor, but wide and pitch will be consistent.Carrier tape is wound or placed on a shipping reel with a diameter of either 330 m m (13 i nches) or 178 m m (7 i nches). The cen-ter hub design is large enough to ensure the radius formed by the carrier tape around it does not put unnecessary stress on the parts.Prior to shipping, moisture sensitive parts (MSL level 2a to 5a) are baked and placed into the pockets of the carrier tape. A cover tape is sealed over the top of the entire length of the carrier tape. The reel is sealed in a moisture barrier, ESD bag, which is placed in a cardboard shipping box. It is important to note that unused moisture sensitive parts need to be resealed in the moisture barrier bag. If the reels exceed the exposure limit and need to be rebaked, most carrier tape and shipping reels are not rate as bakeable at 125°C. If baking is required, devices may be baked according to section 4, table 4-1, column 8 of Joint Industry Standard IPC/JEDEC J-STD-033A.The following table provides useful information for carrier tape and reels used for shipping the devices described in this docu-ment.Carrier Tape Drawing with Part OrientationRF3809RF3809。
VibroFlex QTecPowerful on all surfaces Preliminary datasheetHighlights■Spare performance - SNR improvement up to 20 dB or a factor of 10■Make use of every quantum of light for unparalleled optical sensitivity■High-fidelity data with nosurface preparation − even dark,biological or moving objects ■From μm-sized to large, distant objects■No limits with a high dynamic range up to 30 m/s■Fast remote and auto focus for best signal quality■Match range and depth of field with interchangeable lensesVibroFlex QTecThe Polytec VibroFlex laser Doppler vibrometer is a modular high-performance solution for non-contact vibration measurement. It offers unrivalled measurement performance and versatility for solving pressing vibration issues in both R&D and industrial quality control.The VibroFlex family comprises the front-end VibroFlex Connect and a selection of non-contact laser sensor heads. Integrated with the VibSoft data acquisition and analysis software, the vibration measurement system is ready to go. Study acoustics, dynamics and vibrations on nano to macro structures without contact and with laser precision.The VibroFlex QTec sensor head delivers the highestoptical sensitivity, enabling high-fidelity measurements on all surfaces – even on dark, biological, rotating or moving objects. This safe laser technology is perfect for challenging applications such as NDT, biomedical, long distance displacement measurements, quasi-static displacement measurement and shaker feedback control. QTec makes vibration measurements faster, easier and more reliable than ever – for the most robust, unambiguous results.VibroFlex – the new flexibility of laser vibration measurement.Technical data1Used auto focusrange can be limited individually for shorter cycle time.2Quick and easyoperation of all focus functions with turn-ing knob on sensor head, on touch screen of front-end VibroFlex Connect or remote controlled from a computer or digital device.3Measured from the front edge of the front lens. 4Included with VFX-O-FMI-02 Fiber Lens (IR).5Optional available for VFX-O-FMI-02 Fiber Lens (IR).Options and accessories。
