Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 angstroms 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 angstroms. The crystal structure was solved by molecular-replacement methods. Structure refinement is in progress.
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.,Hilario E, Teixeira EC, Pedroso GA, Bertolini MC, Medrano FJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):446-8. Epub 2006 Apr 12. PMID:16682772[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hilario E, Teixeira EC, Pedroso GA, Bertolini MC, Medrano FJ. 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. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt, 5):446-8. Epub 2006 Apr 12. PMID:16682772 doi:10.1107/S174430910601219X
