Abstract
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
Protein & Peptide Letters
Title: Crystallization and X-Ray Data Analysis of the Extended Dna-Binding Domain of the E2 Bovine Papillomavirus Type 1 Protein
Volume: 8 Issue: 4
Author(s): Joao a.r.g. Barbosa, Carlos Basilio Pinheiro, Adriana C. Alves, Jose R. Brandao neto, Leonardo G. Alonso, Gonzalo de Prat-Gay and Igor Polikarpov
Affiliation:
Keywords: DNA-binding domain, E2 Bovine PapillomaVirus type 1 protein
Abstract: 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.
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Barbosa a.r.g. Joao, Pinheiro Basilio Carlos, Alves C. Adriana, Brandao neto R. Jose, Alonso G. Leonardo, Prat-Gay de Gonzalo and Polikarpov Igor, Crystallization and X-Ray Data Analysis of the Extended Dna-Binding Domain of the E2 Bovine Papillomavirus Type 1 Protein, Protein & Peptide Letters 2001; 8 (4) . https://dx.doi.org/10.2174/0929866013409409
DOI https://dx.doi.org/10.2174/0929866013409409 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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