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


  • 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.

published proceedings

  • Acta Crystallogr D Biol Crystallogr

altmetric score

  • 6

author list (cited authors)

  • Deivanayagam, C. C., Rich, R. L., Danthuluri, S., Owens, R. T., Patti, J. M., Hk, M., DeLucas, L. J., & Narayana, S. V.

citation count

  • 2

complete list of authors

  • Deivanayagam, CC||Rich, RL||Danthuluri, S||Owens, RT||Patti, JM||Höök, M||DeLucas, LJ||Narayana, SV

publication date

  • February 1999