Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris
Journal Article
·
· Acta Crystallographica. Section F
- Institute of Biochemistry, National Chung-Hsing University, Taichung 40227,Taiwan (China)
- Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei,Taiwan (China)
- National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32310 (United States)
- Department of Life Science, National Tsing Hua University, Hsin-Chu,Taiwan (China)
A conserved hypothetical protein XC1692 from X. campestris pv. campestris has been overexpressed in E. coli. The purified recombinant protein crystallized in a variety of forms and diffracted to a resolution of at least 1.45 Å. Xanthomonas campestris pv. campestris strain 17 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, one third of which have no known structure and/or function yet are highly conserved among several different bacterial genuses. One of these gene products is XC1692 protein, containing 141 amino acids. It was overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. The crystals diffract to at least 1.45 Å resolution. They are hexagonal and belong to space group P6{sub 3}, with unit-cell parameters a = b = 56.9, c = 71.0 Å. They contain one molecule per asymmetric unit.
- OSTI ID:
- 22356154
- 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
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