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

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 P2(1)2(1)2(1) with unit-cell parameters a = 39.58, b = 81.39 and c = 112.65 Angstrom. A complete data set was recorded to 2.1 Angstrom resolution and had a V-m of 2.3 Angstrom(3) 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 Angstrom resolution and had unit-cell parameters a = 39.11, b = 81.39 and c = 109.51 Angstrom in the space group P2(1)2(1)2(1) ClfB was crystallized in the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with unit-cell parameters a = 96.31, b = 96.31 and c = 84.13 Angstrom and diffracted to 2.45 Angstrom resolution. The estimated V-m of 2.6 Angstrom(3) Da(-1) with 53% solvent indicated one molecule in the asymmetric unit.