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

doi:10.1107/S0907444998010051

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 Institute

Research output: Contribution to journal › Article

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 language	English (US)
Pages (from-to)	525-527
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	2
DOIs	https://doi.org/10.1107/S0907444998010051
State	Published - Feb 1 1999

ASJC Scopus subject areas

Structural Biology

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Deivanayagam, C. C. S., Rich, R. L., Danthuluri, S., Owens, R. T., Patti, J. M., Hook, M., DeLucas, L. J., & Narayana, S. V. L. (1999). Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein. Acta Crystallographica Section D: Biological Crystallography, 55(2), 525-527. https://doi.org/10.1107/S0907444998010051

Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein. / Deivanayagam, Champion C.S.; Rich, Rebecca L.; Danthuluri, Sita; Owens, Rick T.; Patti, Joseph M.; Hook, Magnus; DeLucas, Lawrence J.; Narayana, Sthanam V.L.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 2, 01.02.1999, p. 525-527.

Research output: Contribution to journal › Article

Deivanayagam, Champion C.S. ; Rich, Rebecca L. ; Danthuluri, Sita ; Owens, Rick T. ; Patti, Joseph M. ; Hook, Magnus ; DeLucas, Lawrence J. ; Narayana, Sthanam V.L. / Crystallization and preliminary X-ray analysis of B-domain fragments of a Staphylococcus aureus collagen-binding protein. In: Acta Crystallographica Section D: Biological Crystallography. 1999 ; Vol. 55, No. 2. pp. 525-527.

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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 {\AA} in either the 1222 or 1212121 space group. These crystals diffracted to 2.5 {\AA} resolution and the calculated V(m) values of 3.2 and 2.2 {\AA}3 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 {\AA} and diffracted to 2.3 {\AA} resolution. For this species, the calculated V(m) value of 2.2 {\AA}3 Da-1 indicates the presence of a monomer in the asymmetric unit.",

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N2 - 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.

AB - 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.

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