Cloning, purification crystallization and preliminary X-ray characterization of a conserved hypothetical protein XC6422 from Xanthomonas campestris

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt 7):703-5. doi: 10.1107/S1744309105019391. Epub 2005 Jun 30.

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 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 x 1.5 x 0.4 mm in size after one week and diffracted to at least 1.6 A 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 A, beta = 109.4 degrees. Determination of this structure may provide insights into the protein's function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / metabolism
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Xanthomonas campestris / genetics
  • Xanthomonas campestris / metabolism*

Substances

  • Bacterial Proteins
  • Recombinant Proteins