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Crystallization and preliminary X-ray diffraction analysis of XAC1151, a small heat-shock protein from Xanthomonas axonopodis pv. citri belonging to the α-crystallin family
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...
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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-05, Vol.62 (5), p.446-448 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | 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 Å 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 Å. The crystal structure was solved by molecular‐replacement methods. Structure refinement is in progress. |
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ISSN: | 1744-3091 1744-3091 |
DOI: | 10.1107/S174430910601219X |