Crystallization and preliminary X-ray diffraction analysis of XAC1151, a small heat-shock protein from Xanthomonas axonopodis pv. citri belonging to the alpha-crystallin family
Nenhuma Miniatura disponível
Data
2006-05-01
Autores
Hilario, E.
Teixeira, E. C.
Pedroso, G. A.
Bertolini, Maria Celia [UNESP]
Medrano, F. J.
Título da Revista
ISSN da Revista
Título de Volume
Editor
Blackwell Publishing
Resumo
The hspA gene (XAC1151) from Xanthomonas axonopodis pv. citri encodes a protein of 158 amino acids that belongs to the small heat-shock protein ( sHSP) family of proteins. These proteins function as molecular chaperones by preventing protein aggregation. The protein was crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium phosphate. X-ray diffraction data were collected to 1.65 angstrom resolution using a synchrotron-radiation source. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 128.7, c = 55.3 angstrom. The crystal structure was solved by molecular-replacement methods. Structure refinement is in progress.
Descrição
Palavras-chave
Como citar
Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 62, p. 446-448, 2006.