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


  • 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.

published proceedings

  • Acta Crystallogr D Biol Crystallogr

author list (cited authors)

  • Deivanayagam, C. C., Perkins, S., Danthuluri, S., Owens, R. T., Bice, T., Nanavathy, T., ... Narayana, S. V.

citation count

  • 14

complete list of authors

  • Deivanayagam, CC||Perkins, S||Danthuluri, S||Owens, RT||Bice, T||Nanavathy, T||Foster, TJ||Höök, M||Narayana, SV

publication date

  • February 1999