Synonyms: None
CsCl
M_r 168.36
CAS Number [7647-17-8]
EC Number 231-600-2
Merck 14,2011
RTECS FK9625000
MDL Number MFCD00010955
PubChem Substance ID 24852585
Purity ≥ 99.5%

Measured pH range: 5.8 – 9.2 at 25°C
Measured Conductivity Range: 111.2 – 114.1 mS/cm at 25°C
Measured Refractive Index Range: 1.34581 – 1.34597 at 20°C

Al  ≤0.0005%
As ≤0.00001%
Ba ≤0.0005%
Bi  ≤0.0005%
Ca ≤0.005%
Cd ≤0.0005%
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%
N  ≤0.001%
Na ≤0.005%
Ni  ≤0.0005%
Pb ≤0.0005%
SO₄ ≤0.002%
Sr  ≤0.0005%
Zn ≤0.0005%

1.0 M Cesium chloride

1. The Three-Dimensional Structure of Ribonuclease-S. H. W. WYCKOFF, D. TSERNOGLOU, A. W. HANSON, J. R. Nox, B. LEE, AND FREDERIC M. RICHARDS. J. Biol. Chem. Wyckoff et al. 245 (2): 305, 1970.

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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Salt is the only primary crystallization reagent (precipitant) utilized. Based on a design of 96 conditions, the screen evaluates a broad portfolio of crystallization salts of varying concentration and pH. The selection, concentration, and pH of the salts were determined by data mining the BMCD¹ and other crystallization databases, crystallization reports in the literature, and internal crystallization trials performed at Hampton Research. Based on this analysis, up to 35% of protein crystallizations involve salt as the primary crystallization reagent. SaltRx can be used as a primary crystallization screen when salt, ionic strength and pH are desired or suspected as appropriate crystallization variables. It is also useful as a secondary screen when salt only reagents/conditions from screens such as Index™, Crystal Screen™, and Grid Screen™ produce crystals and when further screening for additional salt conditions or optimization is desired. Since this screen does not contain volatile organics, it is compatible with microbatch, vapor diffusion, liquid and gel diffusion crystallization methods. SaltRx may also be used for dialysis crystallization in conjunction with Dialysis Buttons™.

The original SaltRx kit (HR2-108) contained 96 unique reagents, 10 ml each. This kit has been discontinued and converted into two 48 reagent based kits, SaltRx 1 and SaltRx 2, available separately, which when used together are identical to the original SaltRx.

SaltRx 1 contains 48 unique reagents, 10 ml each. SaltRx 1 contains reagents 1-48 of the original SaltRx 96 reagent kit.

Salt Rx 2 contains 48 unique reagents, 10 ml each. SaltRx 2 contains reagent 49-96 of the original SaltRx 96 reagent kit.

SaltRx HT contains the 96 SaltRx 1 and SaltRx 2 reagents 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.

Measured pH range of kit is 4.1 to 9.0 at 25°C
Average measured pH of kit is 6.9 at 25°C
Median measured pH of kit is 7.3 at 25°C
Mode measured pH of kit is 7.4 at 25°C

SaltRx 1

SaltRx 2

SaltRx HT

1. Cloning, expression, purification and preliminary X-ray diffraction studies of a mycobacterial protein implicated in bacterial survival in macrophages. A. E. Shahine, P. Y. Chan, D. Littler, J. Vivian, R. Brammananth, P. K. Crellin, R. L. Coppel, J. Rossjohn and T. Beddoe. Acta Cryst. (2013). F69, 566-569.

2. Gilliland, G.L., Tung, M., Blakeslee, D.M. and Ladner, J. 1994. The Biological Macromolecule Crystallization Database, Version 3.0: New Features, Data, and the NASA Archive for Protein Crystal Growth Data. Acta Crystallogr. D50 408-413.

3. Crystallization and preliminary crystallographic analysis of molybdenum-cofactor biosynthesis protein C from Thermus thermophilus. S. P. Kanaujia, C. V. Ranjani, J. Jeyakanthan, S. Baba, L. Chen, Z.-J. Liu, B.-C. Wang, M. Nishida, A. Ebihara, A. Shinkai, S. Kuramitsu, Y. Shiro, K. Sekar and S. Yokoyama. Acta Cryst. (2007). F63, 27-29.

4. Crystal-contact engineering to obtain a crystal form of the Kelch domain of human Keap1 suitable for ligand-soaking experiments. Stefan Horer, Dirk Reinert, Katja Ostmann, Yvette Hoevels and Herbert Nar. Acta Cryst. (2013). F69, 592-596.

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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Duco Cement

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: Cobaltous chloride hexahydrate
Cl₂Co • 6H₂O
M_r 237.93
CAS Number [7791-13-1]
EC Number 231-589-4
Merck 14,2437
RTECS GG0200000
MDL Number MFCD00149652
UN Number UN 3260 8/PG 2
Purity ≥ 98.0%

Appearance (Starting Material): Violet, Crystals
Appearance (Solution): Very deep red

Measured pH Range: 2.1 – 4.6 at 25°C
Measured Conductivity Range: 103.4 – 114.8 mS/cm at 25°C

1.0 M Cobalt(II) chloride hexahydrate

1. Crystallization of tRNA ‘Leu’ from escherichia coli after purification with hydroxyapatite. Spencer, M; Neidle, S; Jones, TA. Biochem Biophys Res Commun 86, 66-70, 1979.

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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Why sitting drop? Placing the droplet in the indentation greatly reduces the risk of losing the protein by accident. Crystallization can be carried out in the presence of detergents and organic solvents which are compatible with polystyrene (such as MPD, iso-propanol, and ethanol). The protein drop is less affected by condensation problems. Soaking and seeding experiments can be carried out easily. Crystals can be transported more securely. Larger drop volumes can be used. Micro-Bridges have a concave indentation in the top surface of the bridge which holds the sample droplet during a crystallization experiment and prevents the droplet from spreading over a large area. Made from polystyrene, these parts are highly transparent and suitable for most crystallizations. The surface of the indentation is highly polished to facilitate the visual inspection of the drops under a microscope. The maximum drop volume for the Micro-Bridge is 35 µl. Reservoirs can be sealed with plain cover slides and vacuum grease or clear sealing tape.

Approximate dimensions: Height: 12 mm Length: 14 mm Width: 7 mm

Micro-Bridges

Micro-Bridges

1. Structure of aluminum-bound ovotransferrin at 2.15 angstrm resolution. K, Mizutani, B. Mikami, S. Aibara, and M. Hirose. Acta Cryst (2005) D61, 1636-1642.

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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MembFac is based upon the highly effective biased sparse matrix methodology. The MembFac screen matrix is optimized for the crystallization of membrane proteins.

MembFac contains 48 unique reagent formulations. With this set of 48 conditions, numerous chemicals and chemical combinations are utilized, allowing one to evaluate a large variety of potential crystallization conditions. MembFac covers a broad pH range between 4 and 9.

The Rationale The basic rationale of MembFac is to perform a sparse matrix screen while changing the detergent dimension because detergents play an important factor in the crystallization of membrane proteins. A MembFac screen is to be completed for each detergent. Detergent screens are available separately.

The Method The membrane protein of interest is first isolated in the detergent which gives the highest stability and activity. The protein concentration should be approximately 10 to 20 mg/ml and the detergent concentration should be only slightly above the CMC. The sample is then set against MembFac, using all 48 solutions plus the screening detergent(s) of choice. The screening detergent concentration should be approximately one to three times the CMC. Hence, for each detergent screened, one would utilize approximately 1 to 2 mg of sample.

The MembFac protocol was used to crystallize membrane proteins including SQR, fumerate: quinone oxireductase, LHII, and LHCII.

Crystal Screen Lite is a sparse matrix of trial crystallization reagent conditions based upon the Crystal Screen™.³ The primary screen variables are salt, pH, and precipitant (salts, polymers, volatile organics, and non-volatile organics).² Crystal Screen Lite differs from the original Crystal Screen kit in that the primary precipitant reagents are one-half the concentration of that used in the original Crystal Screen formulation. The secondary salts, ions, and buffers remain at the original Crystal Screen concentration. Reducing the primary concentration of the primary precipitant results in a screen which is “more gentle” on the sample and typically produces much less precipitate conditions than the original Crystal Screen.

MembFac contains 48 unique reagents, 10 ml each.

MembFac HT contains 1 ml each of all 48 reagents from MembFac and reagents 1-48 from Crystal Screen Lite 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.

MembFac

Crystal Screen Lite

MembFac HT

1. UCLA Crystallization Workshop, June 21, 1993.

2. Crystallization of nucleic acids and proteins, Edited by A. Ducruix and R. Giege, The Practical Approach Series, Oxford Univ. Press, 1992.

3. McPherson, A., Current approaches to macromolecular crystallization., Eur. J. Biochem. (1990) 189, 1-23.

4. Jancarik, J. and Kim, S.H., Sparse Matrix Sampling: a screening method for crystallization of proteins. (1991) J. Appl. Cryst., 24,409-411.

5. Protein and Nucleic Acid Crystallization. Methods, A Companion to Methods in Enzymology, Academic Press, Volume 1, Number 1, August 1990.

6. Structural and functional characterization of the N-terminal domain of the yeast Mg2+ channel Mrs2. M. B. Khan, G. Sponder, B. Sjoblom, S. Svidova, R. J. Schweyen, O. Carugo and K. Djinovic-Carugo. Acta Cryst. (2013). D69, 1653-1664.

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: CTAB, or Cetrimonium bromide or Cetyltrimethylammonium bromide or Palmityltrimethylammonium bromide
C₁₉H₄₂BrN
CH₃(CH₂)₁₅N(Br)(CH₃)₃
M_r 364.45
CAS Number [57-09-0]
EC Number 200-311-3
Beilstein Registry Number 3598189
Merck 14,2025
RTECS BQ7875000
MDL Number MFCD00011772
PubChem Substance ID 24874353
Purity ≥ 99.0%
UN 3077 9/PG 3

Measured pH range: 5.6 – 5.8 at 25°C
Measured Conductivity Range: 1106 – 1174 µS/cm at 25°C
Measured Refractive Index Range: 1.33570 – 1.33575 at 20°C

Solution may form clear, small needle shaped crystals upon cooling to below 25 degrees Celsius. These crystals will dissolve once the solution is warmed to above 25 degrees Celsius and the solution will remain clear once returned to 25 degrees Celsius.

Al  ≤0.0005%
Ba ≤0.0005%
Bi  ≤0.0005%
Ca ≤0.001%
Cd ≤0.0005%
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%

0.05 M Hexadecyltrimethylammonium bromide

1. Crystal Structures of Mycolic Acid Cyclopropane Synthases from Mycobacterium tuberculosis. Chih-chin Huang, Clare V. Smith, Michael S. Glickman, William R. Jacobs Jr., and James C. Sacchettini. J. Biol. Chem., Vol. 277, Issue 13, 11559-11569, March 29, 2002.

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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Micro-Bridges Polypropylene

Micro-Bridges Polypropylene

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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By using sparse matrix sampling technology, The Natrix kits allow one to quickly test wide ranges of pH, salts, and precipitants using a very small sample of nucleic acid.

Natrix screens are unique in that rather than relying solely on the traditional nucleic acid precipitant MPD, Natrix screens also utilize Polyethylene glycols (PEGs) in a variety of molecular weights (200, 400, 4,000, 8,000) as well as 2-Propanol, Polyethylene glycol monomethyl ether (PEG MME), and 1,6-Hexanediol. Many of the polymeric and low molecular weight organic precipitants are combined with various monovalent salts as precipitating agents. This combination of salts and low molecular weight organics and polyalcohols, as well as the utilization of varying chain length PEGs, has proven to be a successful combination for producing nucleic acid and protein-nucleic acid complex crystals.

Natrix contains 48 unique reagents, 10 ml each and is based on the sparse matrix formulation first described by William Scott in 1995.

Natrix 2, an extension of Natrix, contains 48 unique reagents, 10 ml each. Natrix 2 is a biased sparse matrix screen based on extracting patterns from crystallization data as well as reagent formulations first described by Berger et al in 1996.

Natrix HT contains 1 ml of each reagent from Natrix and Natrix 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.

Natrix

Natrix 2

Natrix HT

1. Scott, W. G., Finch, J.T., Grenfell, R., Fogg, J., Smith, T., Gait, M.J., Klug, A., Journal of Molecular Biology (1995) 250: 327-332.

2. Purification, crystallization and preliminary X-ray analysis of the BseCI DNA methyltransferase from Bacillus stearothermophilus in complex with its cognate DNA. E. G. Kapetaniou, D. Kotsifaki, M. Providaki, M. Rina, V. Bouriotis and M. Kokkinidis. Acta Cryst. (2007). F63, 12-14.

3. Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNAGly acceptor-stem microhelix. C. Forster, M. Perbandt, A. B. E. Brauer, S. Brode, J. P. Furste, C. Betzel and V. A. Erdmann. Acta Cryst. (2007). F63, 46-48.

4. Combinatorial crystallization of an RNA-protein complex. Danielle Bodrero Hoggan, Jeffrey A. Chao, G. S. Prasad, C. David Stouta and James R. Williamson. Acta Cryst (2003). D59, 466-473.

5. Cocrystallizing natural RNA with its unnatural mirror image: biochemical and preliminary X-ray diffraction analysis of a 5S rRNA A-helix racemate. Volker A. Erdmanna et al. Acta Cryst. (2007). F63, 839-843.

6. Berger, et al., A Highly Effective 24 Condition Matrix for the Crystallization of Nucleic Acid Fragments. Acta Cryst. Section D. (1996) Vol. D52 Part 3, 465-468.

7. Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNAGly acceptor-stem microhelix. C. Förster, M. Perbandt, A. B. E. Brauer, S. Brode, J. P. Fürste, C. Betzel and V. A. Erdmann. Acta Cryst. (2007). F63, 46-48.

8. Adams, A., Nucleic Acids Research (2002) Vol. 30, 719-725.

9. Preliminary crystallographic analysis of mouse Elf3 C-terminal DNA-binding domain in complex with type II TGF-b receptor promoter DNA. Agarkar et al. Acta Cryst. (2009). F65, 1261-1263.

10. Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+. T.-H. Jang and H. H. Park. Acta Cryst. (2014). F70, 513-516 [ doi:10.1107/S2053230X1400510X ]

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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22 mm OptiClear Plastic circle cover slides

22 mm OptiClear Plastic circle cover slides

22 mm OptiClear Plastic square cover slides

22 mm OptiClear Plastic square cover slides

18 mm OptiClear Plastic circle cover slides

18 mm OptiClear Plastic circle cover slides

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: Ferric chloride hexahydrate
FeCl₃ • 6H₂0
M_r 270.29
CAS Number [10025-77-1]
EC Number 231-729-4
RTECS NO5425000
Merck 14,4019
MDL Number MFCD00149712
PubChem Substance ID 24868480
UN Number 3260 8/PG 3
Purity 98 – 102%

Measured pH range: 0.6 – 1.0 at 25°C
Measured Conductivity Range: 90.0 – 97.8 mS/cm at 25°C

As ≤0.0005%
Ca ≤0.0005%
Cd ≤0.001%
Cl ≤0.002%
Co ≤0.005%
Cr ≤0.01%
Cu ≤0.002%
Fe²⁺ ≤0.002%
K   ≤0.005%
Mg ≤0.001%
Mn ≤0.1%
N   ≤0.001%
Na ≤0.01%
Ni  ≤0.005%
NO₃ ≤0.01%
Pb  ≤0.002%
PO₄ ≤0.01%
SO₄ ≤0.005%
Zn  ≤0.002%

1.0 M Iron(III) chloride hexahydrate

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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