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

Champion C.S. Deivanayagam, Rebecca L. Rich, Sita Danthuluri, Rick T. Owens, Joseph M. Patti, Magnus Hook, Lawrence J. DeLucas, Sthanam V.L. Narayana

Research output: Contribution to journalArticle

2 Scopus citations

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 Å in either the 1222 or 1212121 space group. These crystals diffracted to 2.5 Å resolution and the calculated V(m) values of 3.2 and 2.2 Å3 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 Å and diffracted to 2.3 Å resolution. For this species, the calculated V(m) value of 2.2 Å3 Da-1 indicates the presence of a monomer in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)525-527
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number2
DOIs
StatePublished - Feb 1 1999

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein'. Together they form a unique fingerprint.

Cite this