Currently available screens for protein-nucleic acid complex crystallization rely on the use of additives that may promote the crystallization nucleic acids dissociated from the protein. Thus, these screens can lead to false hits and wasted sample. This screen was designed specifically for protein-nucleic acid complex crystallization. The condition formulations have been developed from an in-depth analysis of actual conditions of existing protein-nucleic acid complexes in the Protein Data Bank (PDB). Through an incomplete factorial method, conditions from the nearly 2,000 deposited protein-nucleic acid complexes were summarized into an extremely efficient 48 condition screen. This screen has been successfully used by the Hollis lab for years.
Protein-Nucleic Acid Complex Crystal Screen Fomulation Table
Please cite the following article when publishing: Pryor EE Jr, Wozniak DJ, Hollis, T. Crystallization of Pseudomonas aeruginosa AmrZ protein: development of a comprehensive method for obtaining and optimization of protein-DNA crystals. Acta Crystallographica Section F. 2012; F68: 985-993.
From the laboratory of Thomas Hollis, PhD, Wake Forest School of Medicine.
Read Dr. Hollis's related blog post, A New Avenue for Protein-Nucleic Acid Complex Crystallization »
Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
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Product Type: | Kit |
Storage: | 4C (short term), -20C (long term) |
Shipped: | Ambient temperature |
Structures solved using Protein-Nucleic Acid Complex Crystal Screen
Transcription factor AmrZ in complex with dsDNA |
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DNA methyl lesion repair enzyme AlkB in complex with ssDNA
PDB ID: 3KHC Holland PJ, Hollis T. Structural and mutational analysis of Escherichia coli AlkB provides insight into substrate specificity and DNA damage searching. PLoS ONE. 2010; 5(1):e8680. |
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3' to 5' exonuclease TREX1 in complex with ssDNA
PDB ID: 2OA8 de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T. The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering. J Biol Chem. 2007; 282(14):10537-43. |
If you publish research with this product, please let us know so we can cite your paper.