Crystallization and preliminary X-ray analysis of XC1015, a histidine triad-like protein from Xanthomonas campestris

Wen Ting Lo, Ko Hsin Chin, Hui Lin Shr, Fei Philip Gao, Ping Chiang Lyu, Andrew H.J. Wang, Shan Ho Chou

研究成果: 雜誌貢獻文章同行評審

摘要

Histidine-triad (HIT) proteins are a superfamily of nucleotide hydrolases and transferases that contain a conserved HφHφHφφ motif (where φ is a hydrophobic amino acid) and are found in a variety of organisms. In addition to binding to a variety of nucleotides, other biological functions of the HIT superfamily proteins have been discovered and HIT malfunction has been implicated in several human diseases. Structural studies of HIT superfamily proteins are thus of particular interest. In this manuscript, the cloning, expression, crystallization and preliminary X-ray analysis of XC1015, a HIT protein present in the plant pathogen Xanthomonas campestris pathovar campestris, are reported. The XC1015 crystals diffracted to a resolution of 1.3 Å. They are tetragonal and belong to space group P432 12, with unit-cell parameters a = 40.52, b = 40.52, c = 126.89 Å.

原文英語
頁(從 - 到)1263-1265
頁數3
期刊Acta Crystallographica Section F: Structural Biology and Crystallization Communications
62
發行號12
DOIs
出版狀態已發佈 - 12月 2006
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 遺傳學
  • 凝聚態物理學

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