JBScreen Nuc-Pro

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, with focus on entries by structural genomic initiatives, the BMCD and other protocols [1-3]. 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

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

Preparation of JBScreen buffers

Products & Ordering

JBScreen Nuc-Pro 1 CS-181

JBScreen Nuc-Pro 2 CS-182

JBScreen Nuc-Pro 3 CS-183

JBScreen Nuc-Pro 4 CS-184

JBScreen Nuc-Pro 1 - 4 CS-185

JBScreen Nuc-Pro HTS CS-209L

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 Nuc-Pro

Dolot et al. (2021) Biochemical, crystallographic and biophysical characterization of histidine triad nucleotide-binding protein 2 with different ligands including a non-hydrolyzable analog of Ap4A. BBA - General Subjects 1865(11):129968.
Alipov et al. (2021) Structure of a Mutant Form of Translation Regulator Hfq with the Extended Loop L4. Crystallography Reports 66:791.
Kim et al. (2020) Ligand binding characteristics of the Ku80 von Willebrand domain. DNA Repair 85:102739.
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.

References and Recommended Reading:

[1] Doudna et al. (1993) Crystallization of ribozymes and small RNA motifs by a sparse matrix approach. Proc. Natl. Sci. USA 90:7829.
[2] Scott et al. (1995) Rapid Crystallization of Chemically Synthesized Hammerhead RNAs using a Double Screening Procedure. J. Mol. Biol. 250:327.
[3] Ke et al. (2004) Crystallization of RNA and RNA-protein complexes. Methods 34:408.