Crystallization And Initial Crystallographic Analysis Of The Streptococcus Parasanguinis Fw213 Fap1-Nr Alpha Adhesive Domain At Ph 5.0

Acta crystallographica. Section F, Structural biology and crystallization communications(2011)

引用 3|浏览5
暂无评分
摘要
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.
更多
查看译文
关键词
x ray diffraction,crystallization
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要