The Crystal Screen and Crystal Screen 2 reagent kits are designed to provide a highly effective and rapid screening method for the crystallization of macromolecules. The screens are simple and practical for finding initial crystallization conditions. The initial crystallization conditions for more than 1,000 proteins, peptides, oligonucleotides, and small molecules have been determined using Crystal Screen.
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.
10 ml, tube format
10 ml, tube format
1 ml, Deep Well block format
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 ]