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Crystallization and Preliminary Crystallographic Study of DNA Polymerase from Pyrococcus furiosus

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A new member of archaeal DNA polymerase from Pyrococcus furiosus was crystallized. Diffraction data to 3.1 Å of the selenomethionine-derivatized crystal were collected, and preliminary crystallographic study has been completed. The crystal belongs to the space group C2 with unit cell parameters of a = 93.2 Å, b = 124.9 Å, c = 87.7 Å, α = 90 , β = 109.7® , and γ = 90 . Assuming the presence of one molecule in the asymmetric unit, the solvent content of the crystal is estimated to be 54%, corresponding to a Matthews coefficient VM of 2.7Å3 Da-1.





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Keywords: DNA polymerase; archaea; crystallization

Document Type: Research Article

Affiliations: Open Laboratory of Advanced Bioscience and Biotechnology (OLABB), Institute for Protein Research, Osaka University. 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.

Publication date: 2007-04-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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