biostudies-literature00600Unknown67(Pt 2)Garnett JAWellcome TrustThe 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(?). Here, Fap1-NR(?) 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.Acta crystallographica. Section F, Structural biology and crystallization communications274-6https://www.ebi.ac.uk/biostudies/studies/S-EPMC3034626biostudies-literatureCrystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NR? adhesive domain at pH 5.0.PMC3034626Tagliaferri CGarnett JARamboarina SWu WLee WCMatthews S60falseCrystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NR? adhesive domain at pH 5.0.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(?). Here, Fap1-NR(?) 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.2011-01-01T00:00:00Z2011 Feb2020-11-19T14:13:29Z2019-03-27T00:01:28ZS-EPMC30346262130110410.1107/s174430911005277210.1107/S1744309110052772