The CrystalCap Vial is a 1.8 ml cryo vial featuring two small vents. A ring magnet is molded into the open end of the vial so that when the cap is positioned in the vial, the ring magnet holds the cap on the vial during cryogenic storage.The HR4-904 CrystalCap Vial does not have a magnet on the bottom of the vial.

The conical shape with ledge is compatible with SSRL style grippers, auto mounters and sample handlers.

Compatible with the following Synchrotron Radiation Beamlines

North & South America
• The Advanced Light Source, Berkeley, California ALS 4.2.2, ALS 11.3.1, ALS 12.2.2, ALS 12.3.2
• The Advanced Photon Source, Argonne, Illinois APS 14-BM-C BioCARS, APS 14-ID-B BioCARS
• Cornell High Energy, Synchrotron Source, Ithaca, New York CHESS A1, CHESS F1
• Canadian Light Source, Saskatchewan, Canada, CLS 08ID-1, CLS 08B1-1
• Stanford Synchrotron Radiation Laboratory, Menlo Park, California SSRL BL7-1, SSRL BL9-1, SSRL BL9-2, SSRL BL11-1, SSRL BL12-2, SSRL BL14-1

Asia & Australia
• Shanghai Synchrotron Radiation Facility, Shanghai, China SSRF BL17U1
• National Synchrotron Radiation Research Center, Taiwan NSRRC BL13B1, NSRRC BL13C1
• Pohang Accelerator Laboratory, Pohang, South Korea PAL 2D, PAL 5C, PAL 7A
• Photon Factory, Tsukuba, Japan PF BL-5A, PF BL-17A, PF AR-NW12A
• Super Photon ring-8 GeV, Japan SPRING-8 BL12B2, SPRING-8 BL24XU, SPRING-8 BL26B1, SPRING-8 BL26B2, SPRING-8 BL32B2, SPRING-8 BL32XU, SPRING-8 BL38B1, SPRING-8 BL41XU, SPRING-8 BL44B2, SPRING-8 BL44XU

CrystalCap

CrystalCap

CrystalCap Vial

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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Synonym: L-(+)-Tartaric acid diammonium salt or Diammonium tartrate
(NH₄)₂C₄H₄O₆
C₄H₁₂N₂O₆
M_r 184.15
CAS Number [3164-29-2]
EC Number 221-618-9
Beilstein Registry Number 6120352
RTECS WW8050000
MDL Number MFCD00013073
PubChem Substance ID 24846510
Purity ≥ 99.5%

HR2-679 Measured pH Range: 6.3 – 6.9 at 25°C
HR2-679 Measured Conductivity Range: 118.2 – 134.4 mS/cm at 25°C
HR2-679 Measured Refractive Index Range: 1.39169 – 1.39346 at 20°C

HR2-767 titrated to pH 7.0 using NaOH at 25°C
HR2-767 Measured Conductivity Range: 115.7 – 129.6 mS/cm at 25°C
HR2-767 Measured Refractive Index Range: 1.38057 – 1.38157 at 20°C

Al  ≤0.0005%
As ≤0.00001%
Ba ≤0.0005%
Bi  ≤0.0005%
Ca ≤0.0005%
Cd ≤0.0005%
Cl  ≤0.005%
Co ≤0.0005%
Cr  ≤0.0005%
Cu ≤0.0005%
Fe  ≤0.0005%
K   ≤0.005%
Li   ≤0.0005%
Mg ≤0.0005%
Mn ≤0.0005%
Mo ≤0.0005%
Na ≤0.005%
Ni  ≤0.0005%
Pb  ≤0.0005%
SO₄ ≤0.005%
Sr  ≤0.0005%
Zn  ≤0.0005%

2.0 M Ammonium tartrate dibasic

1.6 M Ammonium tartrate dibasic pH 7.0

1. Overexpression, crystallization and preliminary X-ray crystallographic analysis of erythronate-4-phosphate dehydrogenase from Pseudomonas aeruginosa. J. Y. Ha, J. H. Lee, K. H. Kim, D. J. Kim, H. H. Lee, H.-K. Kim, H.-J. Yoon and S. W. Suh. Acta Cryst. (2006). F62, 139-141.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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It is designed to evaluate polymer based crystallization reagents and pH in low (PEGRx 1) to medium ionic strength (PEGRx 2). It is also designed for use as a secondary or optimization screen to follow the Hampton Research Index screen when polymer based reagents produce hits and interesting solubility leads.

PEGRx 1 is a crystallization reagent kit designed to evaluate an array of polymers of varying molecular weight in a low ionic strength environment versus a wide range of pH. Polymer reagents include Polyethylene glycols, Polyethylene glycol monomethyl ethers, and Jeffamines^®. The molecular weight range between 200 and 20,000 is evaluated in a low ionic strength formulation. Ten different buffers are used to span the range of pH between 3.5 and 9. The primary screen variables are polymer type, polymer molecular weight, pH and low ionic strength.

PEGRx 2 is a crystallization reagent kit designed to evaluate an array of polymers of varying molecular weight in a medium ionic strength environment in the presence of additives, salts, volatile organics and polyols versus a wide range of pH. Polymer reagents include Polyethylene glycols and Polyethylene glycol monomethyl ethers. The polymer molecular weight range between 200 and 20,000 is evaluated in a medium ionic strength formulation. Ten different buffers are used to span the range of pH between 3.5 and 9. The primary screen variables are polymer type, polymer molecular weight, pH and secondary reagents which include additives, salts, volatile organics and polyols.

PEGRx 1 contains 48 unique reagents, 10 ml each.

PEGRx 2 contains 48 unique reagents, 10 ml each.

PEGRx HT contains the 96 PEGRx 1 and PEGRx 2 reagent in a single Deep Well block format.

Ready-to-use reagents are sterile filtered and formulated with ultra-pure Type 1 water, using the highest purity salts, polymers, organics and buffers. Individual reagents are available through the Hampton Research Custom Shop.

PEGRx 1

PEGRx 2

PEGRx HT

1. Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae. Ae Kyung Park, Seung Min Bong, Jin Ho Moon and Young Min Chi. Acta Cryst. (2009). F65.

2. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors.  Zhang L, Lin D, Sun X, Curth U, Drosten C, Sauerhering L, Becker S, Rox K, Hilgenfeld R. Science. 2020 Apr 24;368(6489):409-412. doi: 10.1126/science.abb3405. Epub 2020 Mar 20.

3. Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.  Zhang, L., Xie, Z., Liu, Z. et al.  Nat Commun 11, 2676 (2020). https://doi.org/10.1038/s41467-020-16500-5.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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CrystalCap ALS (HR4-779) is supplied without a vial (HR4-904).

The CrystalCap Vial is a 1.8 ml cryo vial featuring two small vents. A ring magnet is molded into the open end of the vial so that when the cap is positioned in the vial, the ring magnet holds the cap on the vial during cryogenic storage. The HR4-904 CrystalCap Vial does not have a magnet on the bottom of the vial.

The ledge free conical shape of the CrystalCap ALS is compatible with ALS style grippers, auto mounters and sample handlers.

ALS style sample mounters accept the CrystalCap ALS.

Compatible with the following Synchrotron Radiation Beamlines

North & South America
• The Advanced Light Source, Berkeley, California ALS 4.2.2, ALS 5.0.1, ALS 5.0.2, ALS 5.0.3, ALS 8.2.1, ALS 8.3.1, ALS 11.3.1, ALS 12.2.2, ALS 12.3.2, ALS 12.3.1-APX
• The Advanced Photon Source, Argonne, Illinois APS 14-BM-C BioCARS, APS 14-ID-B BioCARS, APS 17-ID IMCA-CAT, APS 19-BM, APS 19-ID, APS 22-BM SER-CAT, APS 22-ID SER-CAT, PS 23-BM-B GA/CA, APS 23-ID-B GA/CA, APS 23-ID-D GA/CA, APS 24-ID-C NE-CAT, APS 24-ID-E NE-CAT, APS 31-ID LR-CAT
• Center for Advanced Microstructures and Devices, Baton Rouge, Louisiana CAMD GCPCC
• Cornell High Energy, Synchrotron Source, Ithaca, New York CHESS A1, CHESS F1
• Canadian Light Source, Saskatchewan, Canada, CLS 08ID-1, CLS 08B1-1
• The Brazilian Synchrotron, Light Laboratory, Sao Paulo, Brazil LNLS D03B-MX1, LNLS W01B-MX2
• Stanford Synchrotron Radiation Laboratory, Menlo Park, California SSRL BL7-1, SSRL BL9-1, SSRL BL9-2, SSRL BL11-1, SSRL BL12-2, SSRL BL14-1

Europe
• Kurchatov Center for Synchrotron Radiation and Nanotechnology, Moscow, Russia KCSRNT K4.4
• Max-Lab, Lund University, Sweden MAX II I711, MAX II I911-2, MAX II I911-3
• MPG/DESY, Hamburg, Germany MPGDESY BW6
• SOLEIL, Saint-Aubin, France SOLEIL PROXIMA1, SOLEIL PROXIMA2

Asia & Australia
• Shanghai Synchrotron Radiation Facility, Shanghai, China SSRF BL17U1
• National Synchrotron Radiation Research Center, Taiwan NSRRC BL13B1, NSRRC BL13C1
• Pohang Accelerator Laboratory, Pohang, South Korea PAL 2D, PAL 5C, PAL 7A
• Photon Factory, Tsukuba, Japan PF BL-5A, PF BL-17A, PF AR-NW12A • Super Photon ring-8 GeV, Japan SPRING-8 BL12B2, SPRING-8 BL24XU, SPRING-8 BL26B1, SPRING-8 BL26B2, SPRING-8 BL32B2, SPRING-8 BL32XU, SPRING-8 BL38B1, SPRING-8 BL41XU, SPRING-8 BL44B2, SPRING-8 BL44XU

CrystalCap ALS

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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Synonyms: None
CdCl₂ • xH₂O
M_r 183.32
CAS [654054-66-7]
EC Number 233-296-7
Merck 14,1617
UN Number 2570 6.1/PG 3
MDL Number MFCD00149627
PubChem Substance ID 24852504
Purity > 98.0%

Measured pH range: 2.8 – 5.0 at 25°C
Measured Conductivity Range: 26.7 – 28.9 mS/cm at 25°C
Measured Refractive Index Range: 1.35410 – 1.35683 at 20°C

1.0 M Cadmium chloride hydrate

1. Crystallization and preliminary crystallographic data for the Azurin mutant End-121 from Pseudomonas aeruginosa. Strange, RW; Murphy, L; Karlsson, G; Lindley, P; Lundberg, LG; Reinhammar, B; Hasnan, SS. Acta Crystallogr D 50, 37- 39, 1994.

2. Characterization and preliminary attempts for Derivatization of Crystals of Large ribosomal subunits from Haloarcula marismortui diffracting to 3 A resolution. von Bohlen, K; Makowski, I; Hansen, HAS; Bartels, H; Berkovitch-Yellin, Z; Zaytzev-Bashan, A; Meyer, S; Paulke, C; Franceschi, F; Yonath, A. J Mol Biol 222, 11- 15, 1991.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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Using PEG/pH, PEG/pH 2, or PEG/pH HT one isolates pH, buffer type and relative supersaturation from other chemical and physical variables to screen the effect that pH and buffer type have on the solubility, stability, homogeneity, monodispersity and crystallization of the sample. Varying the pH can alter the protonation state and charge of amino acid residues in the protein, generating different species of the protein for solubility and crystallization screening. The change in pH can have a dramatic effect on inter and intramolecular contacts in the protein and can manipulate how the protein interacts with itself, the surrounding solvent and chemicals in the drop. By screening buffer type and pH in a low ionic strength environment of Polyethylene glycol, PEG/pH simultaneously delivers as a solubility and a crystallization screen for proteins.

Designed as a 96 reagent screen, but offered as two sets of 48 x 10 ml reagents or a single 96 x 1 ml reagent block, PEG/pH, PEG/pH 2, and PEG/pH HT samples Polyethylene glycol 4,000 versus 20 different buffers, at 0.2 M, while sampling pH 3.5 – 9.6.

PEG/pH 1 samples 20% w/v Polyethylene glycol 4,000 versus pH 3.5 – 7.4 in 0.2 M buffer. PEG/pH is supplied in a 48 x 10 ml tube format. PEG/pH is compatible with vapor diffusion, free interface diffusion, and microbatch crystallization methods. For research use only.

PEG/pH 2 samples 20% w/v Polyethylene glycol 4,000 versus pH 6.4 – 9.6 in 0.2 M buffer. PEG/pH 2 is supplied in a 48 x 10 ml tube format. PEG/pH 2 is compatible with vapor diffusion, free interface diffusion, and microbatch crystallization methods. For research use only.

PEG/pH HT samples 20% w/v Polyethylene glycol 4,000 versus pH 3.5 – 9.6 in 0.2 M buffer. PEG/pH HT is supplied in a 96 x 1 ml block format. PEG/pH HT is compatible with vapor diffusion, free interface diffusion, and microbatch crystallization methods. For research use only.

PEG/pH

PEG/pH 2

PEG/pH HT

1. Introduction to protein crystallization. Alexander McPherson and Jose A. Gavira. Acta Crystallographica Section F Volume 70, Issue 1, pages 2–20, January 2014.

2. Optimization of crystallization conditions for biological macromolecules. Alexander McPherson and Bob Cudney. Acta Crystallographica Section F Volume 70, Issue 11, pages 1445–1467, November 2014.

3. Protein Isoelectric Point as a Predictor for Increased Crystallization screening efficiency. Katherine A. Kantardjieff and Bernhard Rupp. Bioinformatics (2004) 20.

4. A protein crystallization strategy using automated grid searches on successively finer grid screens. Patricia C. Weber. Methods: A Companion to Methods in Enzymology. Vol. 1, No. 1, August, pp. 31-37, 1990.

5. Two approaches to the rapid screening of crystallization conditions. Alexander McPherson. Journal of Crystal Growth 122 (1992) 161-167.

6. Optimization of buffer solutions for protein crystallization. R. A. Gosavi, T. C. Mueser and C. A. Schall. Acta Cryst. (2008). D64, 506-514.

7. Buffer Solutions The Basics. R.J. Beynon and J.S. Easterby. 1996. IRL Press.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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The CrystalCap Vial is a 1.8 ml cryo vial featuring two small vents. A ring magnet is molded into the open end of the vial so that when the cap is positioned in the vial, the ring magnet holds the cap on the vial during cryogenic storage. The HR4-904 CrystalCap Vial does not have a magnet on the bottom of the vial.

The ledge free conical shape of the CrystalCap ALS HT is compatible with ALS style grippers, auto mounters and sample handlers.

The CrystalCap ALS HT features a two dimensional (2D) alphanumeric 16 x 16 data matrix code on the underside of the cap. Each cap is also color coded for CryoLoop size.

Note: CrystalCap ALS HT with Mounted CryoLoops are sold without vials. Vials HR4-904 sold separately.

Color Coded Cap…………CryoLoop Size
Red…………………………….0.025-0.05 mm
Green…………………………….0.05-0.1 mm
Blue………………………………..0.2-0.3 mm
Blue/Red………………………….0.3-0.4 mm
Green/Red………………………..0.4-0.5 mm
Yellow/Green……………………..0.7-1.0 mm

Compatible with the following Synchrotron Radiation Beamlines

North & South America
• The Advanced Light Source, Berkeley, California ALS 4.2.2, ALS 5.0.1, ALS 5.0.2, ALS 5.0.3, ALS 8.2.1, ALS 8.3.1, ALS 11.3.1, ALS 12.2.2, ALS 12.3.2, ALS 12.3.1-APX
• The Advanced Photon Source, Argonne, Illinois APS 14-BM-C BioCARS, APS 14-ID-B BioCARS, APS 17-ID IMCA-CAT, APS 19-BM, APS 19-ID, APS 22-BM SER-CAT, APS 22-ID SER-CAT, PS 23-BM-B GA/CA, APS 23-ID-B GA/CA, APS 23-ID-D GA/CA, APS 24-ID-C NE-CAT, APS 24-ID-E NE-CAT, APS 31-ID LR-CAT
• Center for Advanced Microstructures and Devices, Baton Rouge, Louisiana CAMD GCPCC
• Cornell High Energy, Synchrotron Source, Ithaca, New York CHESS A1, CHESS F1
• Canadian Light Source, Saskatchewan, Canada, CLS 08ID-1, CLS 08B1-1
• The Brazilian Synchrotron, Light Laboratory, Sao Paulo, Brazil LNLS D03B-MX1, LNLS W01B-MX2
• Stanford Synchrotron Radiation Laboratory, Menlo Park, California SSRL BL7-1, SSRL BL9-1, SSRL BL9-2, SSRL BL11-1, SSRL BL12-2, SSRL BL14-1

Europe
• Kurchatov Center for Synchrotron Radiation and Nanotechnology, Moscow, Russia KCSRNT K4.4
• Max-Lab, Lund University, Sweden MAX II I711, MAX II I911-2, MAX II I911-3
• MPG/DESY, Hamburg, Germany MPGDESY BW6
• SOLEIL, Saint-Aubin, France SOLEIL PROXIMA1, SOLEIL PROXIMA2

Asia & Australia
• Shanghai Synchrotron Radiation Facility, Shanghai, China SSRF BL17U1
• National Synchrotron Radiation Research Center, Taiwan NSRRC BL13B1, NSRRC BL13C1
• Pohang Accelerator Laboratory, Pohang, South Korea PAL 2D, PAL 5C, PAL 7A
• Photon Factory, Tsukuba, Japan PF BL-5A, PF BL-17A, PF AR-NW12A
• Super Photon ring-8 GeV, Japan SPRING-8 BL12B2, SPRING-8 BL24XU, SPRING-8 BL26B1, SPRING-8 BL26B2, SPRING-8 BL32B2, SPRING-8 BL32XU, SPRING-8 BL38B1, SPRING-8 BL41XU, SPRING-8 BL44B2, SPRING-8 BL44XU

CrystalCap ALS HT

CrystalCap ALS HT

CrystalCap ALS HT

CrystalCap ALS HT

CrystalCap ALS HT

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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Synonyms: Cadmium sulfate octahydrate
3CdSO₄ • 8H₂O
3CdO₄S • 8H₂O
M_r 769.52
CAS Number [15244-35-6]
EC Number 233-331-6
Merck 14,1627
RTECS EV2850000
MDL Number MFCD00151655
Purity 98.0% (calc. based on CdSO4 • 8/3 H2O, KT)

Measured pH Range: 1.5 – 2.1 at 25°C
Measured Conductivity Range: 43.6 – 46.5 mS/cm at 25°C
Measured Refractive Index Range: 1.40247 – 1.40679 at 20°C

As  ≤0.0002%
Ca ≤0.005%
Cl  ≤0.001%
Co ≤0.0005%
Cr  ≤0.0005%
Cu ≤0.0005%
Fe  ≤0.0005%
K   ≤0.005%
Mg ≤0.0005%
Mn ≤0.0005%
N   ≤0.003%
Na ≤0.005%
Ni  ≤0.0005%
Pb  ≤0.002%
Zn  ≤0.005%

1.0 M Cadmium sulfate hydrate

1. Selective crystallization of horse isoferritins. Arosio P, Gatti G, Bolognesi M. Biochim Biophys Acta. 1983 Apr 28;744(2):230-2.

2. Ferritin: Its Properties and Significance for Iron Metabolism. S. Granick. Chem. Rev.; 1946; 38(3) pp 379 – 403.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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The primary screening variables are PEG, ion type, ionic strength, and pH. More than 60% of the published crystallizations utilized PEG as a primary crystallization reagent and in approximately 50% of those reports, the PEG was combined with an ion as a secondary crystallization reagent. PEG/Ion reagents are formulated without a buffer and are not pH titrated.

PEG/Ion 2 is an extension to the fundamental crystallization strategy in PEG/Ion. PEG/Ion 2 reagents cover the monodisperse, high purity Polyethylene glycol 3,350 and an array of neutralized and pH adjusted organic acids, multivalent ions, a novel Citrate BIS-TRIS propane buffer system and pH (4 – 8.8). The formulation of PEG/Ion 2 was developed at Hampton Research. Each of the 48 reagents in PEG/Ion 2 contains PEG 3,350 as the polymer (precipitant). The concentration of PEG is varied from 12% w/v to 20% w/v depending upon the type and concentration of buffer/salt paired with the polymer. Thirteen of the forty-eight PEG/Ion 2 reagents contain a separate buffer component. The remaining PEG/Ion 2 reagents are buffered by the titrated organic acid salt. Six of these thirteen conditions feature a novel Citric acid BIS-TRIS propane (CBTP) buffer. The CBTP buffer uses Citric acid and BIS-TRIS propane as the acid base pair to create a two component buffer system effective across pH 2.5 to 9.5. The ratio of Citric acid to BIS-TRIS propane determines the solution pH. Thirty-five of the forty-eight PEG/Ion 2 reagents contain a neutralized or pH adjusted organic acid in the presence of the polymer. Neutralized organic acids are highly effective crystallization salts.¹ Four PEG/Ion 2 reagents feature polyvalent cations. Two of these reagents contain cation mixes, saving sample by screening six different cations with only two reagents. Tryptone, a casein digest combinatorial library of peptides, is included in PEG/Ion 2. PEG/Ion 2 reagents 1-30, 42, 45-47 are formulated without a buffer and are not pH titrated.

PEG/Ion contains 48 unique reagents, 10 ml each.

PEG/Ion 2 contains 48 unique reagents, 10 ml each.

PEG/Ion HT contains 1 ml of each reagent from PEG/Ion and PEG/Ion 2 in a single Deep Well block format.

Ready-to-use reagents are sterile filtered and formulated with ultra-pure Type 1 water, using the highest purity salts, polymers, organics and buffers. Individual reagents are available through the Hampton Research Custom Shop.

PEG/Ion Screen

PEG/Ion 2 Screen

PEG/Ion HT

1. Expression, purification, crystallization and preliminary X-ray diffraction analysis of Bifidobacterium adolescentis xylose isomerase. C. V. dos Reis, A. Bernardes and I. Polikarpov. Acta Cryst. (2013). F69, 588-591.

2. A comparison of salts for the crystallization of macromolecules. Alexander McPherson. Protein Science (2001), 10:418-422.

3. Searching for silver bullets: An alternative strategy for crystallizing macromolecules. Alexander McPherson and Bob Cudney. Journal of Structural Biology Volume 156, Issue 3 , December 2006, Pages 387-406.

4. Mechanisms for Glycolipid Antigen-Driven Cytokine Polarization by Valpha14i NKT Cells. Sulliivan et al, The Journal of Immunology, 2010, 184, 141 -153. (PEG/Ion 2)

5. Optimization of salt concentration in PEG-based crystallization solutions. Yamanaka M, Inaka K, Furubayashi N, Matsushima M, Takahashi S, Tanaka H, Sano S, Sato M, Kobayashi T, Tanaka T. J Synchrotron Radiat. 2011 Jan;18(1):84-7. doi: 10.1107/S0909049510035995. Epub 2010 Nov 5.

6. Crystallization and preliminary X-ray crystallographic analysis of importin-[alpha] from Neurospora crassa. N. E. Bernardes, A. A. S. Takeda, F. Z. Freitas, M. C. Bertolini and M. R. M. Fontes. Acta Cryst. (2014). F70, 501-504 [ doi:10.1107/S2053230X14005068 ]

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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The CrystalCap SPINE Vial is a 1.8 ml cryo vial featuring two small vents and is compatible with the CrystalCap SPINE HT. A ring magnet is molded into the open end of the vial so that when the cap is positioned in the vial, the ring magnet holds the cap on the vial during cryogenic storage. The CrystalCap SPINE Vial features chamfered edges for enhanced cap positioning as well as a magnetic alloy bottom for stability. The HR8-114 CrystalCap SPINE Vial does have a magnet on the bottom of the vial.

The hollowed out design of the CrystalCap SPINE HT is compatible with SPINE style grippers, auto mounters and sample handlers.

The CrystalCap SPINE HT features a two dimensional (2D) alphanumeric 16 x 16 data matrix code on the underside of the cap. Each cap is also color coded for CryoLoop size.

CrystalCap SPINE without 2D code/printing (HR8-094) is the CrystalCap SPINE HT cap only, without 2D code, without color code, without white white background on bottom of cap and no alphanumeric side labeling; cap only, without Mounted CryoLoop.

Note: Caps with Mounted CryoLoops are sold without vials. Vials available separately.

Color Coded Cap…………CryoLoop Size
Red…………………………….0.025-0.05 mm
Green…………………………….0.05-0.1 mm
Yellow………………………………0.1-0.2 mm
Blue………………………………..0.2-0.3 mm
Blue/Red…………………………..0.3-0.4 mm
Green/Red………………………..0.4-0.5 mm
Yellow/Red………………………..0.5-0.7 mm
Yellow/Green……………………..0.7-1.0 mm

Compatible with the following Synchrotron Radiation Beamlines

North & South America
• The Advanced Light Source, Berkeley, California ALS 4.2.2, ALS 11.3.1, ALS 12.2.2, ALS 12.3.2
• The Advanced Photon Source, Argonne, Illinois APS 14-BM-C BioCARS, APS 14-ID-B BioCARS, APS 21-ID-D LS-CAT, APS 21-ID-E LS-CAT, APS 21-ID-F LS-CAT, APS 21-ID-G LS-CAT, APS 23-ID-B GA/CA, APS 23-ID-D GA/CA, APS 24-ID-E NE-CAT, APS 31-ID LR-CAT
• Center for Advanced Microstructures and Devices, Baton Rouge, Louisiana CAMD GCPCC
• Cornell High Energy, Synchrotron Source, Ithaca, New York CHESS A1, CHESS F1
• The Brazilian Synchrotron Light Laboratory, Sao Paulo, Brazil LNLS D03B-MX1, LNLS W01B-MX2
• National Synchrotron Light Source II, Upton, New York NSLS-II 17-ID-1 AMX and NSLS-II 17-ID-2 FMX. NSLS-II 19-ID NYX

Europe
• Cerdanyola del Vallés, Spain ALBA XALOC
• Berlin Electron Storage Ring Company for Synchrotron Radiation, Berlin, Germany BESSY 14.1, BESSY 14.2, BESSY 14.3
• Diamond Light Source, Didcot, Oxfordshire, England DIAMOND I02, DIAMOND I03, DIAMOND I04, DIAMOND I04.1, DIAMOND I24
• Elettra Sincrotrone Trieste, Trieste, Italy ELETTRA 5.2R
• European Molecular Biology Laboratory, Hamburg, Germany EMBL/DESY P13, EMBL/DESY P14
• European Synchrotron Radiation Facility, Grenoble, France ESRF BM14, ESRF BM30A, ID30A-1/MASSIF-1, ID30A-3/MASSIF-3, ESRF ID23-1, ESRF ID23-2, ESRF ID29
• Max-Lab, Lund University, Sweden MAX II I911-2, MAX II I911-3
• Swiss Light Source at Paul Scherer Institut, Switzerland SLS X06DA-PXIII, SLS X06SA-PXI, SLS X10SA-PXII
• SOLEIL, Saint-Aubin, France SOLEIL PROXIMA1, SOLEIL PROXIMA2

Asia & Australia
• Shanghai Synchrotron Radiation Facility, Shanghai, China SSRF BL17U1
• Beijing Synchrotron Radiation Facility, Beijing, China BSRF 1W2B, BSRF 3W1A
• Super Photon ring-8 GeV, Japan SPRING-8 BL12B2, SPRING-8 BL24XU, SPRING-8 BL26B1, SPRING-8 BL26B2, SPRING-8 BL32B2, SPRING-8 BL32XU, SPRING-8 BL38B1, SPRING-8 BL41XU, SPRING-8 BL44B2, SPRING-8 BL44XU

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT

CrystalCap SPINE HT Cap/Vial

CrystalCap SPINE without 2D code/printing

CrystalCap SPINE Vial

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

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Synonyms: Calcium diacetate
(CH₃COO)₂Ca • xH₂O
C₄H₆CaO₄ • xH₂O
M_r 158.17 + aq
CAS Number [114460-21-8]
EC Number 200-540-9
Beilstein Registry Number 3692527
Merck 14,1646
RTECS AF7525000
MDL Number MFCD00150019
PubChem Substance ID 24852644
Purity ≥ 99.0%

Measured pH Range: 7.6 – 7.9 at 25°C
Measured Conductivity range: 34.1 – 38.1 mS/cm at 25°C
Measured Refractive Index range: 1.35697 – 1.35776 at 20°C

As ≤0.00001%
Ba ≤0.0002%
Bi  ≤0.0005%
Cd ≤0.0005%
Cl  ≤0.005%
Co ≤0.0005%
Cr ≤0.0005%
Cu ≤0.0005%
Fe ≤0.0005%
K  ≤0.01%
Li  ≤0.0005%
Mg ≤0.1%
Mn ≤0.0005%
Mo ≤0.0005%
Na ≤0.015%
Ni  ≤0.0005%
Pb ≤0.0005%
SO₄ ≤0.02%
Sr ≤0.02%
Zn ≤0.0005%

1.0 M Calcium acetate hydrate

1. Structure of the B-DNA Decamer C-C-A-A-C-I-T-T-G-G in Two Different Space Groups: Conformational Flexibility of B-DNA. Lipanov, A; Kopka, ML; Kaczor-Grzeskowiak, M; Quintana, J; Dickerson, RE. Biochemistry 32, 1373- 1389, 1993.

Hampton Research, first in crystallization since 1991, developing and delivering crystallization and optimization screens, reagents, plates, and other tools for the crystallization of biological macromolecules, including proteins (antibody), peptides (insulin), and nucleic acids (DNA).

• Products

|

• Gallery

|

• My Account

|

• Contact Us

|

• Quick Order
• Support

• Privacy Policy

|

• Terms and Conditions

• Products

|

• Gallery

|

• My Account

|

• Support

|

• Contact Us

|

• Quick Order

|

• Privacy Policy

|

• Terms and Conditions

© 2022 HAMPTON RESEARCH CORP.

| Website by Skyhound Internet