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


Autoria(s): Hilario, E.; Teixeira, E. C.; Pedroso, G. A.; Bertolini, Maria Celia; Medrano, F. J.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/05/2006

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.

Formato

446-448

Identificador

http://dx.doi.org/10.1107/S174430910601219X

Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 62, p. 446-448, 2006.

1744-3091

http://hdl.handle.net/11449/32886

10.1107/S174430910601219X

WOS:000237159000007

Idioma(s)

eng

Publicador

Blackwell Publishing

Relação

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Direitos

closedAccess

Tipo

info:eu-repo/semantics/article