JBScreen Nuc-Pro
JBScreen Nuc-Pro is designed to screen for preliminary crystallization conditions of nucleic acids and protein-nucleic acid complexes.
Product Information
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).
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 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
- Yin et al. (2017) Impact of cytosine methylation on DNA binding specificities of human transcription factors. Science 356 eaaj2239.
- Nemchinova et al. (2017) An Experimental Tool to Estimate the Probability of a Nucleotide Presence in the Crystal Structures of the Nucleotide–Protein Complexes. Protein J DOI 10.1007/s10930-017-9709-y.
- Wang et al. (2016) Base pairing and structural insights into the 5-formylcytosine in RNA duplex. Nucleic Acids Research 44:4968.
- Nikulin et al. (2016) Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.J Biomol Struct Dyn DOI:10.1080/07391102.2016.1189849.
- 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.