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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/32886
Title: 
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
Author(s): 
Institution: 
  • Ctr Biol Mol Estrrutural
  • Universidade Estadual Paulista (UNESP)
ISSN: 
1744-3091
Abstract: 
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.
Issue Date: 
1-May-2006
Citation: 
Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 62, p. 446-448, 2006.
Time Duration: 
446-448
Publisher: 
Blackwell Publishing
Source: 
http://dx.doi.org/10.1107/S174430910601219X
URI: 
Access Rights: 
Acesso restrito
Type: 
outro
Source:
http://repositorio.unesp.br/handle/11449/32886
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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