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Crystal Screens - JBScreen Nuc-Pro

JBScreen bulk & HTS

JBScreen Nuc-Pro is designed to screen for preliminary crystallization conditions of nucleic acids and protein-nucleic acid complexes.

The highly effective sparse matrix screen is based upon extensive screening of the PDB [1], with focus on entries by structural genomic initiatives, the BMCD [2] and other protocols [3-5]. Reported crystallization conditions for various RNAs, DNAs as well as protein-nucleic acid complexes were compiled and analyzed for rate of recurrence.
The 96 conditions selected cover a variety of polymers, mono- and divalent metal ions, organics, alcohols and buffers of a pH range from 4,0 to 8,5. The organization of the reagents into individual kits is based upon the main precipitant, i.e. various molecular weight PEGs, Salts, alcohols (MPD and 2-Propanol).


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

The ready-to-use reagents are tested for DNase contamination using our DNase Detection Kit → Molecular Biology.


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

References and Recommended Reading:

[1] Berman et al. (2000) The Protein Data Bank. Nucleic Acids Research 28:235.
[2] Gilliland et al. (1994) The Biological Macromolecule Crystallization Database, Version 3.0: New Features, Data, and the NASA Archive for Protein Crystal Growth Data. Acta Cryst. D50:408.
[3] Doudna et al. (1993) Crystallization of ribozymes and small RNA motifs by a sparse matrix approach. Proc. Natl. Sci. USA 90:7829.
[4] Scott et al. (1995) Rapid Crystallization of Chemically Synthesized Hammerhead RNAs using a Double Screening Procedure. J. Mol. Biol. 250:327.
[5] Ke et al. (2004) Crystallization of RNA and RNA-protein complexes. Methods 34:408.

Selected Literature Citations of JBScreen Nuc-Pro

  • Morgunova et al. (2015) Structural insights into the DNA-binding specificity of E2F family transcription factors. Nat. Commun. DOI:10.1038/ncomms10050.
  • Tishchenko et al. (2013) Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gao-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036. Acta Cryst. F 69:61.