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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].

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.


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


BIOZ Product Citations

Please click the arrow on the right to expand the citation list. Click publication title for the full text.

Further Selected Literature Citations of JBScreen JCSG++

  • Talens-Perales et al. (2021) Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity. Computational and Structural Biotechnology Journal 19:2676.
  • Ebner et al. (2021) A Helminth-Derived Chitinase Structurally Similar to Mammalian Chitinase Displays Immunomodulatory Properties in Inflammatory Lung Disease. Journal of Immunology Research Vol. 2021, Article ID 6234836.
  • Giunta et al. (2020) Tuning the Properties of Natural Promiscuous Enzymes by Engineering Their Nano-environment. ACS Nano 14:17652.
  • Bonn-Breach et al. (2019) Structure of Sonic Hedgehog protein in complex with zinc(II) and magnesium(II) reveals ion-coordination plasticity relevant to peptide drug design. Acta Cryst D 75:969.
  • McDougall et al. (2019) Proteinaceous Nano container Encapsulate Polycyclic Aromatic Hydrocarbons. Sci. Rep. 9:1058.
  • De Wijn et al. (2018) Combining crystallogenesis methods to produce diffraction-quality crystals of a psychrophilic tRNA-maturation enzyme. Acta Cryst F 74:747.
  • Kumar et al. (2018) Novel insights into the degradation of β-1,3-glucans by the cellulosome of Clostridium thermocellum revealed by structure and function studies of a family 81 glycoside hydrolase. Int. J. Biol. Macromol. 117:890.
  • Leal et al. (2018) Crystal structure of DlyL, a mannose-specific lectin from Dioclea lasiophylla Mart. Ex Benth seeds that display cytotoxic effects against C6 glioma cells. Int. J. Biol. Macromol. 114:64.
  • Sousa Cavada et al. (2018) Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential. Int. J. Biol. Macromolec. 106:369.
  • Ernst et al. (2018) A comparative structural analysis of the surface properties of asco-laccases. PLOS ONE DOI:10.1371/journal.pone.0206589.
  • Kumar et al. (2017) Non-classical transpeptidases yield insight into new antibacterials. Nat. Chem. Biol. 13:54.
  • Nascimento et al. (2017) Structural analysis of Dioclea lasiocarpa lectin: A C6 cells apoptosis-inducing protein. Int. J. Biochem. Cell Biol. 92:79.
  • 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.


[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.