SaltRx 1 #01 / SaltRx HT A1 185ml

SaltRx 1 #02 / SaltRx HT A2 185ml

SaltRx 1 #03 / SaltRx HT A3 185ml

SaltRx 1 #04 / SaltRx HT A4 185ml

SaltRx 1 #05 / SaltRx HT A5 185ml

SaltRx 1 #06 / SaltRx HT A6 185ml

SaltRx 1 #07 / SaltRx HT A7 185ml

SaltRx 1 #08 / SaltRx HT A8 185ml

SaltRx 1 #09 / SaltRx HT A9 185ml

SaltRx 1 #10 / SaltRx HT A10 185ml

SaltRx 1 #11 / SaltRx HT A11 185ml

SaltRx 1 #12 / SaltRx HT A12 185ml

SaltRx 1 #13 / SaltRx HT B1 185ml

SaltRx 1 #14 / SaltRx HT B2 185ml

SaltRx 1 #15 / SaltRx HT B3 185ml

SaltRx 1 #16 / SaltRx HT B4 185ml

SaltRx 1 #17 / SaltRx HT B5 185ml

SaltRx 1 #18 / SaltRx HT B6 185ml

SaltRx 1 #19 / SaltRx HT B7 185ml

SaltRx 1 #20 / SaltRx HT B8 185ml

SaltRx 1 #21 / SaltRx HT B9 185ml

SaltRx 1 #22 / SaltRx HT B10 185ml

SaltRx 1 #23 / SaltRx HT B11 185ml

SaltRx 1 #24 / SaltRx HT B12 185ml

SaltRx 1 #25 / SaltRx HT C1 185ml

SaltRx 1 #26 / SaltRx HT C2 185ml

SaltRx 1 #27 / SaltRx HT C3 185ml

SaltRx 1 #28 / SaltRx HT C4 185ml

SaltRx 1 #29 / SaltRx HT C5 185ml

SaltRx 1 #30 / SaltRx HT C6 185ml

SaltRx 1 #31 / SaltRx HT C7 185ml

SaltRx 1 #32 / SaltRx HT C8 185ml

SaltRx 1 #33 / SaltRx HT C9 185ml

SaltRx 1 #34 / SaltRx HT C10 185ml

SaltRx 1 #35 / SaltRx HT C11 185ml

SaltRx 1 #36 / SaltRx HT C12 185ml

SaltRx 1 #37 / SaltRx HT D1 185ml

SaltRx 1 #38 / SaltRx HT D2 185ml

SaltRx 1 #39 / SaltRx HT D3 185ml

SaltRx 1 #40 / SaltRx HT D4 185ml

SaltRx 1 #41 / SaltRx HT D5 185ml

SaltRx 1 #42 / SaltRx HT D6 185ml

SaltRx 1 #43 / SaltRx HT D7 185ml

SaltRx 1 #44 / SaltRx HT D8 185ml

SaltRx 1 #45 / SaltRx HT D9 185ml

SaltRx 1 #46 / SaltRx HT D10 185ml

SaltRx 1 #47 / SaltRx HT D11 185ml

SaltRx 1 #48 / SaltRx HT D12 185ml

SaltRx 2 #01 / SaltRx HT E1 185ml

SaltRx 2 #02 / SaltRx HT E2 185ml

SaltRx 2 #03 / SaltRx HT E3 185ml

SaltRx 2 #04 / SaltRx HT E4 185ml

SaltRx 2 #05 / SaltRx HT E5 185ml

SaltRx 2 #06 / SaltRx HT E6 185ml

SaltRx 2 #07 / SaltRx HT E7 185ml

SaltRx 2 #08 / SaltRx HT E8 185ml

SaltRx 2 #09 / SaltRx HT E9 185ml

SaltRx 2 #10 / SaltRx HT E10 185ml

SaltRx 2 #11 / SaltRx HT E11 185ml

SaltRx 2 #12 / SaltRx HT E12 185ml

SaltRx 2 #13 / SaltRx HT F1 185ml

SaltRx 2 #14 / SaltRx HT F2 185ml

SaltRx 2 #15 / SaltRx HT F3 185ml

SaltRx 2 #16 / SaltRx HT F4 185ml

SaltRx 2 #17 / SaltRx HT F5 185ml

SaltRx 2 #18 / SaltRx HT F6 185ml

SaltRx 2 #19 / SaltRx HT F7 185ml

SaltRx 2 #20 / SaltRx HT F8 185ml

SaltRx 2 #21 / SaltRx HT F9 185ml

SaltRx 2 #22 / SaltRx HT F10 185ml

SaltRx 2 #23 / SaltRx HT F11 185ml

SaltRx 2 #24 / SaltRx HT F12 185ml

SaltRx 2 #25 / SaltRx HT G1 185ml

SaltRx 2 #26 / SaltRx HT G2 185ml

SaltRx 2 #27 / SaltRx HT G3 185ml

SaltRx 2 #28 / SaltRx HT G4 185ml

SaltRx 2 #29 / SaltRx HT G5 185ml

SaltRx 2 #30 / SaltRx HT G6 185ml

SaltRx 2 #31 / SaltRx HT G7 185ml

SaltRx 2 #32 / SaltRx HT G8 185ml

SaltRx 2 #33 / SaltRx HT G9 185ml

SaltRx 2 #34 / SaltRx HT G10 185ml

SaltRx 2 #35 / SaltRx HT G11 185ml

SaltRx 2 #36 / SaltRx HT G12 185ml

SaltRx 2 #37 / SaltRx HT H1 185ml

SaltRx 2 #38 / SaltRx HT H2 185ml

SaltRx 2 #39 / SaltRx HT H3 185ml

SaltRx 2 #40 / SaltRx HT H4 185ml

SaltRx 2 #41 / SaltRx HT H5 185ml

SaltRx 2 #42 / SaltRx HT H6 185ml

SaltRx 2 #43 / SaltRx HT H7 185ml

SaltRx 2 #44 / SaltRx HT H8 185ml

SaltRx 2 #45 / SaltRx HT H9 185ml

SaltRx 2 #46 / SaltRx HT H10 185ml

SaltRx 2 #47 / SaltRx HT H11 185ml

SaltRx 2 #48 / SaltRx HT H12 185ml

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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These reagents can perturb and manipulate sample-sample and sample-solvent interactions, as well as perturb water structure which can alter and improve both the solubility and crystallization of a sample. Additives can stabilize or engender conformity by specific interaction with the macromolecules. There are numerous reports of the use of additives to improve the quality and size of macromolecular crystals.^1-5

Additive screen reagent classifications include multivalent, salt, amino acid, dissociating agent, linker, polyamine, osmolyte, chaotrope, co-factor, reducing agent, chelating agent, polymer, carbohydrate, non-detergent, amphiphile, detergent, non-volatile organic and volatile organic.

Additive Screen contains 96 unique reagents, 1 ml each.

Additive Screen HT contains 96 unique reagents, 1 ml each, in a single Deep Well block.

Additive Screen

Additive Screen HT

1. Crystallization of membrane proteins., Edited by Hartmut Michel, CRC Press (1991).

2. Crystallization of Nucleic Acids and Proteins: A Practical Approach., Edited by A. Ducruix and R. Giege, Oxford University Press (1992).

3. Cudney, R., et al., Screening and optimization strategies for macromolecular crystal growth., Acta Cryst. (1994) D50, 414-423.

4. Sousa R., Use of glycerol, polyols and other protein structure stabilizing agents in protein crystallization., Acta Cryst. (1995) D51, 271-277.

5. Trakhanov, S. and Quiocho, F.A., Influence of divalent cations on protein crystallization., Protein Science (1995) 4, 9, 1914-1919.

6. Crystallization and preliminary X-ray diffraction analysis of YhbJ from Escherichia coli, a key protein involved in the GlmYZ sRNA regulatory cascade. M. Resch, Y. Gopel, B. Gorke and R. Ficner. M. Resch, Y. Gopel, B. Gorke and R. Ficner.

7. 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.

8. Thermofluor-based optimization strategy for the stabilization and crystallization of Campylobacter jejuni desulforubrerythrin. Santos SP, Bandeiras TM, Pinto AF, Teixeira M, Carrondo MA, Romão CV. Protein Expr Purif. 2012 Feb;81(2):193-200. doi: 10.1016/j.pep.2011.10.001. Epub 2011 Oct 24. (Thermofluor using the Additive Screen)

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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A highly effective approach to overcome the exhaustive search for suitable crystallization conditions is the use of a sparse matrix method of trial conditions that is biased and selected from known crystallization conditions for macromolecules. The formulation utilized in Crystal Screen and Crystal Screen 2 evaluates 96 unique mixtures of pH, salts, polymers and organics, and their ability to promote crystal growth. 

Crystal Screen contains 50 unique reagents, 10 ml each and is based on the sparse matrix formulation first described by Jancarik and Kim in 1991.

Crystal Screen 2, an extension of Crystal Screen, contains 48 unique reagents, 10 ml each and is based on the formulation first described by Cudney et al in 1994.

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

Crystal Screen

Crystal Screen 2

Crystal Screen HT

1. Jancarik, J. & Kim, S.H. J. Appl. Cryst. 24, 409-411, (1991).

2. Cudney, R., Patel, S., Weisgraber, K., Newhouse, Y., and McPherson, A., Acta Cryst. (1994) D50, 414-423.

3. Expression, purification, crystallization and preliminary X-ray analysis of two arginine-biosynthetic enzymes from Mycobacterium tuberculosis. F. Moradian, C. Garen, L. Cherney, M. Cherney and M. N. G. James. Acta Cryst. (2006). F62, 986-988.

4. The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images. McFerrin and Snell, J. Appl. Cryst. (2002). 35, 538-545.

5. Get phases from arsenic anomalous scattering: de novo SAD phasing of two protein structures crystallized in cacodylate buffer. Liu X, Zhang H, Wang XJ, Li LF, Su XD. PLoS One. 2011;6(9):e24227. Epub 2011 Sep 2.

6. Cloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction-modification enzyme from Vibrio vulnificus. L. Huynh Thi Yen, S.-Y. Park and J.-S. Kim. Acta Cryst. (2014). F70, 489-492 [ doi:10.1107/S2053230X14004543 ]

7. Crystallization and preliminary X-ray analysis of a novel type of lipolytic hydrolase from Bacillus licheniformis. H. Ju, R. Pandian, K. Kim, K. K. Kim and T. D. Kim. Acta Cryst. (2014). F70, 473-475 [ doi:10.1107/S2053230X14004142 ]

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 Crystal Screen Cryo kits removes the guess work from determining the preliminary glycerol concentration required to mix with the crystallization reagent to form an amorphous glass. Crystal Screen Cryo reagents are formulated with the appropriate amount of glycerol required to form an amorphous glass with each unique reagent composition. Crystals obtained in Crystal Screen Cryo kits will already have a suitable concentration of glycerol in the reagent. This avoids exhaustive empirical searches for preliminary cryoprotectant conditions. From the preliminary cryoprotectant conditions, cryoprotectant concentration can be optimized to minimize mosaic spread and maximize diffraction resolution. 

Crystal Screen Cryo kits are biased sparse matrices designed for rapid screening of crystallization conditions of biological macromolecules in the presence of glycerol, the most frequently utilized cryoprotectant. The Crystal Screen Cryo kits utilize the original Crystal Screen™ and Crystal Screen 2™ protocol optimized to include the appropriate concentration of glycerol required to form an amorphous glass at 100°K. The primary screen variables are salt, pH, precipitant (salts, polymers, volatile organics, and non-volatile organics), and cryoprotectant concentration. The screen is a straightforward, effective, and practical kit for determining preliminary crystallization conditions and provides a good starting point for finding suitable cryoprotectant conditions for macromolecular crystals grown in a wide range of reagents. Crystal Screen Cryo is also effective in determining the solubility of a macromolecule in a wide range of precipitants and pH.

Crystal Screen Cryo contains 50 unique reagents, 10 ml each and is based on the sparse matrix formulation first described by Jancarik and Kim in 1991 and refined for cryo by Garman in 1996.

Crystal Screen 2 Cryo contains 48 unique reagents, 10 ml each and is based on the formulation first described by Cudney et al in 1994 and refined for cryo by Snell et al in 2002.

Crystal Screen Cryo HT contains 1 ml each of reagents 1-48 from Crystal Screen Cryo and 48 reagents from Crystal Screen 2 Cryo 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.

Crystal Screen Cryo

Crystal Screen 2 Cryo

Crystal Screen Cryo HT

1. Garman, E.F. and Mitchell, E.P., J. Appl. Cryst. (1996) 29, 584- 587.

2. Structure of the single-stranded DNA-binding protein from Streptomyces coelicolor. Stefanic et al, Acta Cryst. (2009) D65, 974-979.

3. The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images. McFerrin and Snell, J. Appl. Cryst. (2002). 35, 538-545.

4. Cudney, R., Patel, S., Weisgraber, K., Newhouse, Y., and McPherson, A., Acta Cryst. (1994) D50, 414-423.

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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For crystallization to take place, a protein must be soluble in aqueous solution. Ideally the sample should be homogeneous, monodisperse, and in a state of aggregation conducive to interactions which will promote the nucleation and subsequent growth of a crystal. Unfavorable aggregation can compete with, obstruct, and prevent the normal ordering or the sample into a crystal. Many proteins, typically membrane proteins, membrane associated proteins, and soluble proteins contain hydrophobic residues on the surface which can lead to non-specific aggregation, a deterrent to solubility and crystallization. Mild, biological detergents can perturb and manipulate hydrophobic sample-sample and sample-solvent interactions. Incorporating detergents into the solubilization or crystallization reagent during screening and optimization is a popular and effective strategy for identifying conditions which promote and enhance solubility and crystallization. Besides improving the crystallization properties for some proteins and nucleic acids, detergents have also been shown to alleviate problems of twinning and secondary nucleation and can also produce different crystal forms.

Since it can be difficult to impossible a priori to predict and select which detergent or solubilizing agent will minimize the general nonspecific interactions yet at the same time sustain the specific interactions necessary for crystallization, the screening of a portfolio of detergent and solubilizing reagents is an efficient and effective strategy to identify the appropriate and best detergent reagent. The Detergent Screen is a set of solubilization and crystallization specific, mild, biological detergent reagents in a ready to use format at concentrations appropriate for solubility and crystallization screens. The Detergent Screen format allows one to identify a detergent effect as well as help select the best detergent reagent.

Each Detergent Screen kit contains 96 unique detergents. 0.25 ml of detergent solution is formulated at 10 times the reported CMC (unless otherwise noted) in sterile filtered deionized water. The Detergent Screen kit contains 96 solutions in a single Deep Well block, a single sheet of AlumaSeal II Sealing Film, User Guide, Formulations, and Scoring Sheet.

Detergent Screen

1. Protein crystallogra phy with non detergent sulfobetaines. Laurent Vuillard, Bassem Baalbakia, Mogens Lehmanna, Sofie Norager, Pierre Legrand, Michel Roth. 1996, J Cryst Growth 168 150-154.

2. A defined protein–detergent–lipid complex for crystallization of integral membrane proteins: The cytochrome b6f complex of oxygenic photosynthesis. Huamin Zhang, Genji Kurisu, Janet L. Smith, and William A. Cramer. Proc Natl Acad Sci U S A. 2003 April 29, 100(9): 5160–5163.

3. An experiment regarding crystalliza tion of soluble proteins in the pres-ence of b-octyl-glucoside. McPherson A., Koszelak, S., Axelrod, H., Day, J., Williams, R., McGrath, M., Robinson, L., and Cascio, D. 1986, J. Biol. Chem. 261: 1969.

4. McPherson A. (1999). Crystallization of Biological Macromolecules. Cold Spring Harbor Laboratory Press, 253-258.

5. Crystallization of membrane proteins. Edited by Hartmut Michel, CRC Press, 1991.

6. Crystallization of nucleic acids and proteins, Edited by A. Ducruix and R. Giege, The Practical Approach Series, Oxford Univ. Press, 1992 175-191.

7. The effects of neutral detergents on the crystallization of soluble proteins. A. McPherson et al. 1986, J. Crystal Growth, 76, 547-553.

8. Kuhlbrand, W., Quarterly Rev. Biophys., 21, 429, 1988.

9. Garavito, R.M., & Picot, D., Methods, A Companion to Methods in En-zymology, 1, 57, 1990.

10. The growth and characterization of membrane protein crystals. R. Mi-chael Garavito, Zora Markovic-Housley, John A. Jenkins. 1986, Journal of Crystal Growth, 76, 701-709.

11. Screening and optimization strategies for macromolecular crystal growth. R. Cudney, S. Patel, K. Weisgraber, Y. Newhouse and A. McPherson. 1994, Acta Cryst. D50, 414-423.

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 chemicals in GRAS Additive have been used under one or more of the following categories. As (1) a Generally Recognized As Safe (GRAS) substance, (2) a pharmaceutical excipient, (3) a normal physiological constituent, (4) a metabolic byproduct.⁵, and/or (5) a Everything Added to Food in the United States (EAFUS) substance.

The 96 by 1 ml, deep well block reagent screen, is designed to be compatible with most popular crystallization reagents including reagents utilized in Hampton Research screens. Compatible with vapor diffusion, microbatch, and free interface diffusion. For research use only.

GRAS Additive

1. Searching for silver bullets: An alternative strategy for crystallizing macromolecules. Alexander McPherson and Bob Cudney. Journal of Structural Biology 156 (2006) 387-406.

2. A novel strategy for the crystallization of proteins: X-ray diffraction validation. Steven B. Larson, John S. Day, Robert Cudney, and Alexander McPherson. Acta Cryst. (2007) D63, 310-318.

3. Development of an alternative approach to protein crystallization. McPherson, Alexander; Nguyen, Chieniang; Larson, Steven B; Day, John S; Cudney, Bob. J Struct Funct Genomics, Volume 8, Number 4, December 2007, 193-198.

4. Progress in the Development of an Alternative Approach to Macromolecular Crystallization. S. B. Larson,J. S. Day, C. Nguyen, R. Cudney, and A. McPherson. Crystal Growth & Design 2008 Volume 8, No. 8 3038-3052.

5. Wishart DS, Jewison T, Guo AC, Wilson M, Knox C, et al., HMDB 3.0 – The Human Metabolome Database in 2013. Nucleic Acids Res. 2013. Jan 1;41(D1):D801-7. 23161693.

6. 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.

7. Screening and optimization strategies for macromolecular crystal growth. Cudney R, Patel S, Weisgraber K, Newhouse Y, McPherson A. Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):414-23.

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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Heavy Atom Screen Pt

Heavy Atom Screen Au

Heavy Atom Screen Hg

Heavy Atom Screen M1

Heavy Atom Screen M2

1. Towards a rational approach for heavy-atom derivative screening in protein crystallography. Johnson Agniswamy, M. Gordon Joyce, Carl H. Hammer, and Peter D. Sun. Acta Cryst. (2008) D64, 354-367.

2. Heavy-atom derivatization. Elspeth Garman and James W. Murray, Acta Cryst. (2003). D59, 1903-1913.

3. Screening for phasing atoms in protein crystallography. Titus J Boggon and Lawrence Shapiro. Structure 2000, Vol 8 No 7, 143-149.

4. Generating isomorphous heavy-atom derivatives by a quick-soak method. Part II: phasing of new structures. Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1099-103. Epub 2002 Jun 20. Sun PD, Radaev S.

5. Generating isomorphous heavy-atom derivatives by a quick-soak method. Part I: test cases. Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1092-8. Epub 2002 Jun 20. Sun PD, Radaev S, Kattah M.

6. Preparation of isomorphous heavy-atom derivatives. Methods Enzymol. 1985;114:147-56. Petsko GA. PMID: 4079763

7. An overview of heavy-atom derivatization of protein crystals. A. C. W. Pike, E. F. Garman, T. Krojer, F. von Delft & E. P. Carpenter (2016). Acta Cryst. D72, 303-318.

8. Fluorescence Detection of Heavy Atom Labeling (FD-HAL): a rapid method for identifying covalently modified cysteine residues by phasing atoms.Chaptal V, Ujwal R, Nie Y, Watanabe A, Kwon S, Abramson J. J Struct Biol. 2010 Jul;171(1):82-7.

9. A rapid and rational approach to generating isomorphous heavy-atom phasing derivatives. Lu J, Sun PD. FEBS J. 2014 Sep;281(18):4021-8.

10. A rational approach to heavy-atom derivative screening. Joyce MG, Radaev S, Sun PD. Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):358-65.

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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Index, as the name implies, efficiently samples a series of specially formulated reagent zones to identify which reagent class or classes and pH are effective in producing crystals or limiting sample solubility. Results from Index can be used to design optimization experiments and to identify follow on screens by reagent class. For example, positive results with salt based reagents in Index may be followed up with further screening using SaltRx or Grid Screen Salt HT. Success with polymer based reagents in Index may be followed up with further screening using PEGRx or PEG/Ion.

Index utilizes a broad, yet refined portfolio of crystallization reagent systems. These include the following: (1) traditional salts such as Ammonium sulfate and Sodium chloride versus pH; (2) neutralized organic acids such as Sodium malonate and Tacsimate; (3) High salt concentration mixed with low polymer concentration as well as high polymer concentration mixed with low salt concentration and; (4) Low ionic strength using polymers such as PEG, MPD, Pentaerythritols versus pH. These reagent systems are formulated across a sparse matrix and incomplete factorial of concentration ranges, sampling a pH range of 3 to 9.

Index contains 96 unique reagents, 10 ml each.

Index HT contains 96 unique 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 3 to 9 at 25°C
Average measured pH of kit is 6.8 at 25°C
Median measured pH of kit is 6.9 at 25°C

Index

Index HT

1. The advantages of using a modified microbatch method for rapid screening of protein crystallization conditions. A. D′Arcy, A. Mac Sweeney, M. Stihle and A. Haber. Acta Cryst. (2003). D59, 396-399.

2. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium. D. K. Simanshu and M. R. N. Murthy. Acta Cryst. (2005). F61, 52-55.

3. Preparation, crystallization and preliminary X-ray analysis of the methionine synthase (MetE) from Streptococcus mutans. T.-M. Fu, X.-Y. Zhang, L.-F. Li, Y.-H. Liang and X.-D. Su. Acta Cryst. (2006). F62, 984-985.

4. Crystallization and preliminary X-ray analysis of glutathione transferases from cyanobacteria. S. C. Feil, J. Tang, G. Hansen, M. A. Gorman, E. Wiktelius, G. Stenberg and M. W. Parker. Acta Cryst. (2009). F65, 475-477.

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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Ionic liquids have been found effective as additives in protein crystallization, with different ionic liquids used to increase crystallization rates and crystal size.^1-4 The inclusion of ionic liquids in crystallization experiments has been reported to lead to less crystal polymorphism as well as less precipitation at higher precipitant concentrations.²⁵ Ionic liquids have been used as additives to produce crystals in reagents that had previously not resulted in crystallization and results suggest ionic liquids may be applicable for the solubilization and crystallization of membrane proteins.²

Ionic liquids are organic salts with melting points below 100°Celsius. They are thermally stable, nonflammable and demonstrate very low vapor pressure. Ionic liquids are soluble in a variety of organic and inorganic reagents and can be highly water soluble. Ionic liquids can demonstrate a degree of localized structuring about each ion compared to materials composed of disassociated ions, setting them apart from salt solutions.^5-6 Ionic liquids can participate in ionic, hydrophobic and hydrogen bond interactions. Ionic liquids are often chaotropic, composed of low symmetry ions with charge delocalization and weak intermolecular interactions.¹ These organic salts generally consist of combinations of organic cations and either an organic or inorganic anion. Ionic liquids have been demonstrated to suppress protein aggregation and significantly increase protein folding yields.^7-8 Ionic liquids have been reported to stabilize protein activity and structure.^9-11 The inclusion of the ionic liquid 1-n-Butyl-3-methylimidazolium tetrafluoroborate (included in this kit) improved the thermal stability and solubility of integral membrane proteins for membrane proteomics study.¹²

Some ionic liquids, such as ethylammonium nitrate have water-like characteristics, including the capacity for hydrogen bonding and the promotion of micelle formation by some surfactants.¹³ Many ionic liquids are also organics acids and have ionic character in addition to the hydrophobic behavior, which makes them unique and useful solvents in protein chemistry.

Variation of the anion and the cation as well as the utilization of both soft (formate and acetate) and hard anions (nitrate) in the Ionic Liquid Screen reagents provides an additional dimension for evaluating the effects on ionic liquids on the solubility and crystallization of proteins. The Ionic Liquid Screen contains a set of 24 water soluble ionic liquids that comprise different cation (imidazolium, phosphonium, ammonium) and anion (borate, halides, sulfates, acetates, sulfonates, nitrates) structures for a diverse ionic liquid additive screen for use in improving the crystallization behavior and X-ray diffraction resolution of proteins.

Each of the 24 ionic liquids are preformulated in deionized water and sterile filtered using a 0.2 micron filter. Ionic liquid Screen contains 24 unique reagents, 0.5 milliliter each.

Ionic Liquid Screen

1. Pusey, M.L., Paley, M.S., Turner, M.B., and Rogers, R.D. 2007. Protein crystallization using room temperature ionic liquids. Crystal Growth & Design. 74:787-793.

2. Hekmat, D., Hebel, D., Sebastian, J. Schmidt, M., and Weuster-Botz, D. 2007. Advanced protein crystallization using water-soluble ionic liquids as crystallization additives. Biotech. Lett., 29:703-1711.

3. Garlitz, J.A., Summers, C.A., Flowers, R.A. and Borgstahl, G.E.O. 1999. Ethylammonium nitrate: A protein crystallization reagent. Acta Cryst. D53:2037-2038.

4. Judge, R.A., Takahashi, S., Longnecker, K.L. Fry, E.H., Abad-Zapatero, C., and Chi, M.L. 2009. The effects of ionic liquids on protein crystallization and X-ray diffraction resolution. Crystal Growth & Design 9:3463-3469.

5. Bowran, D.T., Hardacre, C. Holbrey, J.D., McMath, J.E., and Soper, A.K. 2003. J. Chem. Phys. 118:173-178.

6. Cadena, C., Zhao, Q., Snurr, and R.Q., Maginn, E.J. 2006. J. Chem. Phys. B 110:2821-2832.

7. Summers, C.A. and Flowers, R.A. 2000. Protein renaturation by the liquid organic salt ethylammonium nitrate. Protein Science 9:2001-2008.

8. Lange, C., Patil, G., and Rudolph, R. 2005. Ionic liquids as refolding additives: N′-alkyl and N′-(w-hydroxyalkyl) N-methylimidazolium chloride. Protein Science 14:2693-2701.

9. Lozano, P. , de Diego, T. Guegan, J.P., Vaultier, M., and Ibora, J.L. 2001. Stabilization of a-chymotrypsin by ionic liquids in transesterification reactions. Biotehnol. Bioeng. 75:363-369.

10. Baker, S.N., McCleskey, T.M., Pandy, S., and Baker, G.A. 2004. Fluorescence study of protein thermostability in ionic liquids. Chem. Commun. 2004:940-941.

11. De Diego, T., Lozano, P., Gmouth, S. Vaultier, M., and Iborra, J.L. 2004. Fluorescence and CD spectroscopic analysis of the a-chymotrypsin stabilization by the ionic liquid 1-ethyl-3-methyimidazolium bis[(trifluormethyl)sulfonyl]amide. Biotechnol. Bioeng. 88:916-924.

12. Sun, L., Tao, D., Han, B., Ma, J., Zhu, G., Liang, Z., Shan, Y., Zhang, L., and Zhang, Y. 2010. Ionic liquid 1-butyl-3-methyl imidazolium tetrafluoroborate for shotgun membrane proteomics. Anal. Bioanal. Chem. DOI 10.1007/s0216-010-4381-5.

13. Evans, D.F., Yamauchi, A., Roman, R., and Casassa, E.Z. 1982. J. Colloids Interface Sci. 88:89-96.

14. Proteins in Ionic Liquids: Current Status of Experiments and Simulations. Christian Schrode, Top Curr Chem (J). 2017; 375(2): 25.

15. Ionic Liquids as Stabilization and Refolding Additives and Solvents for Proteins. Fujita K. Adv Biochem Eng Biotechnol. 2018 Jul 13. doi: 10.1007/10_2018_65.

16. Fujita K. (2018) Ionic Liquids as Stabilization and Refolding Additives and Solvents for Proteins. In: . Advances in Biochemical Engineering/Biotechnology. Springer, Berlin, Heidelberg.

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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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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The PCT kit contains 4 unique, preformulated, sterile filtered reagents used to evaluate protein concentration for crystallization screening. Initially, the sample protein is mixed with two of the reagents to determine if the protein concentration is appropriate for crystallization screening. If the protein is very sensitive to salt and polymer concentration, based on initial PCT results, the protein may be evaluated using a second set of PCT reagents. PCT results will then provide insight to either the appropriate sample concentration or indicate that other diagnostic testing such as native gel electrophoresis or dynamic light scattering should be performed to demonstrate sample homogeneity appropriate for crystallization.

PCT Kit comparison table.

PCT (with slides)

PCT (reagents only)

PCT (with plates and slides)

PCT (with plates and slides)

1. Crystallization and x-ray diffraction analysis of human CLEC-2. Aleksandra A. Watson and Christopher A. O’Callaghan. Acta Cryst. (2005). F61, 1094-1096.

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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Most G protein-coupled receptors (GPCRs) have been crystallized in Polyethylene glycol (PEG) 400 based reagents¹. PEG/Ion 400 is designed as a 96 reagent crystallization screen that is compatible with the Lipidic Cubic Phase (LCP).

PEG/Ion 400 is supplied in a sterile, polypropylene 96 Deep Well block, each reservoir containing 1 ml of sterile filtered reagent. The block is compatible with robotic and multi-channel pipet liquid handling systems and is heat sealed using a special polypropylene backed film. Each PEG/Ion 400 is supplied with an adhesive sealing film which can be used to seal the block after removing the heat seal.

The screen combines a single concentration (30% v/v) of high purity Polyethylene glycol 400 and 48 different high purity salts, comprising both anions (malate, malonate, nitrate, phosphate, succinate, sulfate, tartrate, and thiocyanate) and cations (ammonium, cadmium, calcium, ethylammonium, lithium, magnesium, nickel, potassium, sodium, tetraethylammonium, and zinc) in two concentrations (0.1 and 0.4 M) which due to their unique pH characteristics also affords a reasonable pH screen (approximate pH range of 4 to 9.5). The primary screen variables are PEG, ion type, ionic strength, salt concentration, and pH.

PEG/Ion 400

1. Successful Strategies to Determine High-Resolution Structures of GPCRs. Xiang J, Chun E, Liu C, Jing L, Al-Sahouri Z, Zhu L, Liu W. Trends Pharmacol Sci. 2016 Dec;37(12):1055-1069.

2. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Kang Y, Zhou XE, Gao X, et al. Nature. 2015;523(7562):561-567. doi:10.1038/nature14656.

3. Development of an Automated High Throughput LCP-FRAP Assay to Guide Membrane Protein Crystallization in Lipid Mesophases. Fei Xu, Wei Liu, Michael A. Hanson, Raymond C. Stevens, and Vadim Cherezov. Cryst. Growth Des., 2011, 11 (4), pp 1193-1201.

4. A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes. Martin Caffrey. Acta Crystallogr F Struct Biol Commun. 2015 Jan 1; 71(Pt 1): 3-18.

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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