首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Purification crystallization and halide phasing of a Streptococcus agalactiae backbone pilin GBS80 fragment
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Purification crystallization and halide phasing of a Streptococcus agalactiae backbone pilin GBS80 fragment

机译:无乳链球菌主链菌毛蛋白GBS80片段的纯化结晶和卤化物定相

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摘要

The Gram-positive pathogen Streptococcus agalactiae or group B streptococcus (GBS) is the leading cause of bacterial septicemia, pneumonia and meningitis among neonates around the world. The pathogen assembles two types of pili on its surface, named PI-1 and PI-2, that mediate bacterial adherence to host cells. The GBS PI-1 pilus is formed by the major pilin GBS80, which forms the pilus shaft, and two minor pilins GBS104 and GBS52, which are incorporated into the pilus structure. While considerable structural information exists on Gram-negative pili, the structural study of Gram-positive pili is an emerging area of research. Here, the purification, crystallization and initial phasing of the 35 kDa major fragment of the backbone pilin GBS80 are reported. Crystals were obtained in two different space groups: P21 and C2. SAD data collected from an iodide-derivative crystal at the home source were used to obtain initial phases and interpretable electron-density maps.
机译:革兰氏阳性病原体无乳链球菌或B组链球菌(GBS)是全球新生儿细菌性败血症,肺炎和脑膜炎的主要原因。病原体在其表面上组装了两种类型的菌毛,分别称为PI-1和PI-2,它们介导细菌与宿主细胞的粘附。 GBS PI-1菌毛由构成菌毛柄的主要菌毛GBS80和结合在菌毛结构中的两个小菌毛GBS104和GBS52组成。尽管革兰氏阴性菌毛有大量的结构信息,但革兰氏阳性菌毛的结构研究是一个新兴的研究领域。在此,报道了骨架菌毛蛋白GBS80的35 kDa主要片段的纯化,结晶和初步定相。在两个不同的空间组中获得了晶体:P21和C2。从本地来源的碘化物衍生物晶体收集的SAD数据用于获得初始相和可解释的电子密度图。

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