JBScreen JCSG ++

JBScreen JCSG++ is a sparse matrix screen optimized for initial screening of crystallization conditions of biological macromolecules. The screen has been formulated by researchers from the Joint Center for Structural Genomics (JCSG) [1] and from the European Genomics Consortium [2].

Full Description
SKU: M-CS-151$291.00
SKU: M-CS-152$291.00
SKU: M-CS-153$291.00
SKU: M-CS-154$291.00
SKU: M-CS-155$949.00
SKU: M-CS-206L$437.00

Product Information

JBScreen JCSG++ is a sparse matrix screen optimized for initial screening of crystallization conditions of biological macromolecules. The screen has been formulated by researchers from the Joint Center for Structural Genomics (JCSG) [1] and from the European Genomics Consortium [2].

96 reagents have been selected with the aim to maximize the coverage of the crystallization parameter space and to reduce the redundancy of crystallization conditions within commercially available crystallization screens. Thus, a core set of 66 conditions used by the JCSG for high-throughput structural determination [1] was extended to 96 screening conditions in order to round off the pH profile and to incorporate different precipitants such as succinate, malonate and formate.

When JBScreen JCSG++ is used along with JBScreen PACT++, the benefits of a sparse matrix screen can be combined with the systematic investigation the precipitation behaviour of the protein.

Format

Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well

References

[1] Page et al. (2004) Shotgun crystallization strategy for structural genomics: an optimized two-tiered crystallization screen against the Thermotoga maritima proteome. Acta Cryst. D 59:1028.
[2] Newman et al. (2005) Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy. Acta Cryst. D 61:1426.

Selected Literature Citations of JBScreen JCSG++

Kumar et al. (2017) Non-classical transpeptidases yield insight into new antibacterials. Nat. Chem. Biol. 13:54.
Cattani et al. (2015) Structure of a PEGylated protein reveals a highly porous double-helical assembly. Nat. Chem. 7:823.
Boltsis et al. (2014) Non-contact Current Transfer Induces the Formation and Improves the X‑ray Diffraction Quality of Protein Crystals. Crystal Growth & Design 14:4347.