Products > Crystallization Screens > Red Wings Screen HT > Red Wings Screen HT
Red Wings Screen HT
Applications
- Primary screen for proteins, soluble peptides, nucleic acids, & water soluble small molecules
- Sparse matrix additive screen
Features
- Sparse matrix formula efficiently samples salts, polymers, organics, & pH
- Deep Well block format
Description
Red Wings Screen HT offers a sparse matrix of trial crystallization reagent conditions based upon the original Red Wings Screen of Alexei Savchenko’s Group while at Structural Proteomics in Toronto.3 The screen was developed during the protein structure initiative period (2000 to 2015) of structural genomics. Red Wings Screen became part of the high throughput protein crystallization process at the Structural Genomics Consortium during that time. The primary screen variables are salt, pH, and precipitant (salts, polymers, volatile organics, and non-volatile organics).
Red Wings Screen HT is supplied in a sterile, polypropylene 96 Deep Well block, each reservoir containing 1 ml of reagent. The block is heat sealed using a special polypropylene backed film. Each Red Wings Screen HT kit is supplied with an adhesive sealing film which can be used to seal the block after removing the heat seal. Additional adhesive sealing films can be obtained from Hampton Research or laboratory supply companies which offer high throughput plates and seals.
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.
Support Material(s)
HR2-073 Red Wings Screen HT Documents
Red Wings Screen HT Formulation & Scoring HR2-073 Red Wings Screen HT SDS
References
1. Crystallization of nucleic acids and proteins, Edited by A. Ducruix and R. Giege, The Practical Approach Series, Oxford Univ. Press, 1992.
2. Current approaches to macromolecular crystallization. McPherson, A. Eur. J. Biochem. 189, 1-23, 1990.
3. Salvage or recovery of failed targets by in situ proteolysis. Yufeng Tong, Aiping Dong, Xiaohui Xu, Amy Wernimont. Methods Mol Biol. 2014;1140:179- 88. doi: 10.1007/978-1-4939-0354-2_14.
4. Protein and Nucleic Acid Crystallization. Methods, A Companion to Methods in Enzymology, Academic Press, Volume 1, Number 1, August 1990.
