Cloning, purification crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC6422 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 XC6422 from X. campestris pv. campestris has been overexpressed in E. coli, purified and crystallized. Crystals obtained from the purified recombinant protein showed a variety of forms that diffracted to at least 1.6 Å resolution. 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 genes of unknown function are highly conserved among several different bacterial genuses. XC6422 is one such conserved hypothetical protein and has been overexpressed in Escherichia coli, purified and crystallized in a variety of forms using the hanging-drop vapour-diffusion method. Crystals grew to approximately 2 × 1.5 × 0.4 mm in size after one week and diffracted to at least 1.6 Å resolution. They belong to the monoclinic space group C2, with one molecule per asymmetric unit and unit-cell parameters a = 75.8, b = 79.3, c = 38.2 Å, β = 109.4°. Determination of this structure may provide insights into the protein’s function.
- OSTI ID:
- 22356147
- 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
Similar Records
Preparation, crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC1692 from Xanthomonas campestris
Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestris
Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris
Journal Article
·
Fri Jul 01 00:00:00 EDT 2005
· Acta Crystallographica. Section F
·
OSTI ID:22356154
Cloning, purification, crystallization and preliminary X-ray analysis of XC229, a conserved hypothetical protein from Xanthomonas campestris
Journal Article
·
Fri Jul 01 00:00:00 EDT 2005
· Acta Crystallographica. Section F
·
OSTI ID:22356138
Preparation, crystallization and preliminary X-ray analysis of XC2382, an ApaG protein of unknown structure from Xanthomonas campestris
Journal Article
·
Fri Jul 01 00:00:00 EDT 2005
· Acta Crystallographica. Section F
·
OSTI ID:22356136