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Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of YopM, an essential virulence factor extruded by the plague bacterium Yersinia pestis

  1. Author:
    Evdokimov, A. G.
    Anderson, D. E.
    Routzahn, K. M.
    Waugh, D. S.

  2. Author Address

    NCI, Prot Engn Sect, Frederick Canc Res & Dev Ctr, POB B, Frederick, MD 21702 USA. NCI, Prot Engn Sect, Frederick Canc Res & Dev Ctr, Frederick, MD 21702 USA. NCI, Struct Biol Core Facil, Program Struct Biol, Frederick Canc Res & Dev Ctr, Frederick, MD 21702 USA.
    1. Year: 2000
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 56
    2. 12
    3. Pages: 1676-1679
  4. Type of Article: Article
  1. Abstract:

    A recombinant form of Yersinia pestis YopM with a C-terminal polyhistidine affinity tag has been overproduced in Escherichia coli, purified to homogeneity and crystallized using the hanging-drop vapor-diffusion technique. Several different crystal forms were obtained. The most suitable crystals for X- ray diffraction belonged to space groups P4(2)22 (unit-cell parameters a = 109.36, b = 109.36, c = 101.50 Angstrom) and C222(1) (unit-cell parameters a = 71.73, b = 121.85, c = 189.79 Angstrom). With a synchrotron-radiation source, these crystals diffracted to 2.4 and 1.9 Angstrom resolution, respectively.

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