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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


Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.


[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++

  • 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.