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

类别：结晶筛
产品信息
产品描述
规格 – 屏幕条件
JBScreen JCSG++是一种针对生物大分子结晶条件的初步筛选而优化的稀疏矩阵筛选器。该筛选由结构基因组学联合中心 (JCSG) [1] 和欧洲基因组学联盟 [2] 的研究人员制定。
选择了 96 种试剂，目的是最大限度地扩大结晶参数空间的覆盖范围，并减少市售结晶屏幕中结晶条件的冗余。因此，JCSG 用于高通量结构测定的 66 个核心条件 [1] 扩展到 96 个筛选条件，以完善 pH 曲线并加入不同的沉淀剂，如琥珀酸盐、丙二酸盐和甲酸盐。

当 JBScreen JCSG++ 与 JBScreen PACT++ 一起使用时，稀疏矩阵筛选的好处可以与蛋白质沉淀行为的系统研究相结合。

格式

散装 – 24 或 96 种筛查溶液，10 毫升等分试样
HTS – 96 种筛选溶液以深孔模块形式提供，每孔 1.7 ml

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.

Download technical sheet from below:JBScreen JCSG++ 1 JBScreen JCSG++ 2 JBScreen JCSG++ 3 JBScreen JCSG++ 4 JBScreen JCSG++ HTS L