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Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system

  • Author(s) / Creator(s)
  • TraF, a component of the Escherichia coli type IV secretory system, has been crystallized and preliminary X-ray diffraction data have been collected. TraF is a 26 kDa protein encoded by the E. coli F plasmid and is required for conjugative plasmid transfer and the formation of sex pili. The N-terminal domain of TraF has no recognizable sequence features, whereas the C-terminal domain is believed to adopt a thioredoxin fold. However, since the active-site cysteines of thioredoxin-like proteins are not conserved in TraF, its biochemical role remains unclear. TraF crystallizes in space group C2, with unit-cell parameters a = 119.87, b = 34.36, c = 46.21 A, β= 90.40°, and crystals diffract to 2.3 A resolution.

  • Date created
    2004
  • Subjects / Keywords
  • Type of Item
    Article (Published)
  • DOI
    https://doi.org/10.7939/R3HH6CH1Q
  • License
    © 2004 International Union of Crystallography
  • Language
  • Citation for previous publication
    • GF Audette, SJ Holland, J Manchak, K Hayakawa, LS Frost and B Hazes. "Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system." Acta Crystallographica Section D Biological Crystallography 60 (2004): 2025-2027.