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Crystallization and X-Ray Data Analysis of the Extended Dna-Binding Domain of the E2 Bovine Papillomavirus Type 1 Protein

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Hanging-drop vapour-diffusion method was used for the crystallization of the extended DNA-binding domain (residues 309-410) of the E2 protein from Bovine Papillomavirus Type 1. X-ray data collection at 2.0 A resolution was performed using synchrotron radiation. The crystal symmetry could be described by the space group P3121 and with unit cell parameters a = b = 55.3 A, c = 203.4 A. The protein structure was solved by molecular replacement.

Keywords: DNA-binding domain; E2 Bovine PapillomaVirus type 1 protein

Document Type: Review Article


Publication date: 2001-08-01

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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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