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

Journal Article · · Acta Crystallographica. Section F
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  1. Institute of Biochemistry, National Chung-Hsing University, Taichung 40227,Taiwan (China)
  2. Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei,Taiwan (China)
  3. Department of Life Science, National Tsing Hua University, Hsin-Chu,Taiwan (China)
A conserved hypothetical protein XC229 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. A crystal of the purified recombinant protein diffracted to a resolution of 1.80 Å. 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 I2{sub x}3, with unit-cell parameters a = b = c = 106.8 Å. It contains one or two molecules per asymmetric unit.
OSTI ID:
22356138
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English