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Crystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1 - NRα adhesive domain at pH 5.0

Research output: Contribution to journalArticle

James A. Garnett, Stéphanie Ramboarina, Wei Chao Lee, Camille Tagliaferri, Wilfred Wu, Stephen Matthews

Original languageEnglish
Pages (from-to)274-276
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number2
DOIs
Publication statusPublished - 1 Feb 2011

King's Authors

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-NRα has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution. The crystals belonged to space group P41212 or P4 3212, 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.

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