Crystallization of ClfA and ClfB fragments: the fibrinogen-binding surface proteins of Staphylococcus aureus.

Academic Article

Abstract

  • Recombinant constructs encoding the fibrinogen-binding domains of ClfA and ClfB from Staphylococcus aureus have been crystallized. ClfA was crystallized in the orthorhombic space group P212121 with unit-cell parameters a = 39.58, b = 81.39 and c = 112.65 A. A complete data set was recorded to 2.1 A resolution and had a Vm of 2. 3 A3 Da-1 with 46.5% solvent, suggesting one molecule per asymmetric unit. Co-crystals of ClfA with the 17 amino-acid C-terminal peptide of fibrinogen gamma-chain diffracted to 2.1 A resolution and had unit-cell parameters a = 39.11, b = 81.39 and c = 109.51 A in the space group P212121. ClfB was crystallized in the tetragonal space group P41212 or P43212 with unit-cell parameters a = 96.31, b = 96. 31 and c = 84.13 A and diffracted to 2.45 A resolution. The estimated Vm of 2.6 A3 Da-1 with 53% solvent indicated one molecule in the asymmetric unit.
  • Keywords

  • Amino Acid Sequence, Bacterial Proteins, Crystallization, Crystallography, X-Ray, Fibrinogen, Membrane Proteins, Molecular Sequence Data, Peptide Fragments, Protein Binding, Protein Conformation, Staphylococcus aureus
  • Author List

  • Deivanayagam CC; Perkins S; Danthuluri S; Owens RT; Bice T; Nanavathy T; Foster TJ; Höök M; Narayana SV
  • Start Page

  • 554
  • End Page

  • 556
  • Volume

  • 55
  • Issue

  • Pt 2