title: Crystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NRα adhesive domain at pH 5.0.
abstract: The adhesin fimbriae-associated protein 1 (Fap1) is a surface protein of Streptococcus parasanguinis FW213 and plays a major role in the formation of dental plaque in humans. Increased adherence is highly correlated to a reduction in pH and acid activation has been mapped to a subdomain: Fap1-NR(α). Here, Fap1-NR(α) has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 122.0, c = 117.8 Å. It was not possible to conclusively determine the number of molecules in the asymmetric unit and heavy-atom derivatives are now being prepared.
authors.affiliation: Centre for Structural Biology, Division of Molecular Biosciences, Department of Life Sciences, Imperial College London, London, England.
authors.forename: James A
authors.initials: JA
authors.lastname: Garnett
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Ramboarina
authors.forename: Wei-chao
authors.initials: WC
authors.lastname: Lee
authors.forename: Camille
authors.initials: C
authors.lastname: Tagliaferri
authors.forename: Wilfred
authors.initials: W
authors.lastname: Wu
authors.forename: Stephen
authors.initials: S
authors.lastname: Matthews
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D036781:Fimbriae Proteins / Q000737:chemistry*; D010861:Fimbriae, Bacterial; D006801:Humans; D006863:Hydrogen-Ion Concentration; D014961:X-Ray Diffraction
chemical_list: C403708:fap1 protein, Streptococcus; D036781:Fimbriae Proteins