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