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A pivotal role for reductive methylation in the de novo crystallization of a ternary complex composed of Yersinia pestis virulence factors YopN, SycN and YSc

  1. Author:
    Schubot, F. D.
    Waugh, D. S.

  2. Author Address

    NCI, Prot Engn Sect, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA Waugh, DS, NCI, Prot Engn Sect, Macromol Crystallog Lab, Ctr Canc Res, POB B, Frederick, MD 21702 USA
    1. Year: 2004
    2. Date: NOV
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 60
    2. Part 11
    3. Pages: 1981-1986
  4. Type of Article: Article
  1. Abstract:

    Structural studies of a ternary complex composed of the Yersina pestis virulence factors YopN, SycN and YscB were initially hampered by poor solubility of the individual proteins. Co-expression of all three proteins in Escherichia coli yielded a well behaved complex, but this sample proved to be recalcitrant to crystallization. As crystallization efforts remained fruitless, even after the proteolysis-guided engineering of a truncated YopN polypeptide, reductive methylation of lysine residues was employed to alter the surface properties of the complex. The methylated complex yielded crystals that diffracted X-rays to a maximal resolution of 1.8 Angstrom. The potential utility of reductive methylation as a remedial strategy for high-throughput structural biology was further underscored by the successful modi cation of a selenomethionine-substituted sample

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  1. View record in Web of Science®
  2. WOS: 000224595200008

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