Crystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NRα adhesive domain at pH 5.0
Crystallization and initial crystallographic analysis of the Streptococcus parasanguinis FW213 Fap1-NRα adhesive domain at pH 5.0
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DOI：
10.1107/s1744309110052772
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发表时间：
2011-02-01
影响因子：
0.9
通讯作者：
Matthews, Stephen
中科院分区：
文献类型：
--
作者：
Garnett, James A.;Ramboarina, Stephanie;Matthews, Stephen
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 alpha. Here, Fap1-NR alpha has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 angstrom 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 angstrom. It was not possible to conclusively determine the number of molecules in the asymmetric unit and heavy-atom derivatives are now being prepared.
