Crystallization and X-Ray Data Analysis of the Extended Dna-Binding Domain of the E2 Bovine Papillomavirus Type 1 Protein
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 describe...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2001 |
| País: | Argentina |
| Institución: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositorio: | CONICET Digital (CONICET) |
| Idioma: | inglés |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/45198 |
| Acceso en línea: | http://hdl.handle.net/11336/45198 |
| Access Level: | acceso abierto |
| Palabra clave: | Dna-Binding Domaine Papillomavirus https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| Sumario: | 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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