Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestris

Ko Hsin Chin, Wei Tien Kuo, Chia Cheng Chou, Hui Lin Shr, Ping Chiang Lyu, Andrew H.J. Wang, Shan Ho Chou

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Xanthomonas campestris pv. campestris is a Gram-negative yellow-pigmented pathogenic bacterium that causes black rot, one of the major worldwide diseases of cruciferous crops. Its genome contains approximately 4500 genes, roughly one third of which have no known structure and/or function. However, some of these unknown genes are highly conserved among several different bacterial genuses. XC229 is one such protein containing 134 amino acids. It was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystal diffracted to a resolution of at least 1.80 Å. It is cubic and belongs to space group I2x3, with unit-cell parameters a = b = c = 106.8 Å. It contains one or two molecules per asymmetric unit.

Original languageEnglish
Pages (from-to)694-696
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number7
DOIs
Publication statusPublished - Jul 2005
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Fingerprint

Dive into the research topics of 'Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestris'. Together they form a unique fingerprint.

Cite this