Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein.

Academic Article

Abstract

  • Recombinant proteins of monomeric and dimeric B-domain repeats of a Staphylococcus aureus FDA 574 collagen-binding adhesin have been crystallized. The single repeat unit (B1) was crystallized in a body-centered orthorhombic lattice with a = 96.9, b = 101.3, c = 120. 8 A in either the I222 or I212121 space group. These crystals diffracted to 2.5 A resolution and the calculated Vm values of 3.2 and 2.2 A3 Da-1 suggest the possibility of a dimer or a trimer in the asymmetric unit. The two-repeat fragment (B1B2) crystallized in the orthorhombic space group P212121 with cell dimensions a = 42.4, b = 79.4, c = 130.4 A and diffracted to 2.3 A resolution. For this species, the calculated Vm value of 2.2 A3 Da-1 indicates the presence of a monomer in the asymmetric unit.
  • Keywords

  • Carrier Proteins, Crystallization, Crystallography, X-Ray, Integrins, Protein Conformation, Receptors, Collagen, Recombinant Proteins, Staphylococcus aureus
  • Author List

  • Deivanayagam CC; Rich RL; Danthuluri S; Owens RT; Patti JM; Höök M; DeLucas LJ; Narayana SV
  • Start Page

  • 525
  • End Page

  • 527
  • Volume

  • 55
  • Issue

  • Pt 2