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
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/05/2006
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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 |