首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre
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Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre

机译:噬菌体T5 L形纤维C端结构域的结晶

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摘要

Tails of bacteriophage T5 (a member of the Siphoviridae family) were studied by electron microscopy. For the distal parts of the L-shaped tail fibres, which are involved in host cell receptor binding, a low-resolution volume was calculated. Several C-terminal fragments of the fibre were expressed and purified. Crystals of two of them were obtained that belonged to space groups P6(3) and R32 and diffracted synchrotron radiation to 2.3 and 2.9 angstrom resolution, respectively. A single-wavelength anomalous dispersion data set to 2.5 angstrom resolution was also collected from a selenomethionine-derivatized crystal of one of the fragments, which belonged to space group C2.
机译:通过电子显微镜研究了噬菌体T5的尾巴(Siphoviridae家族的成员)。对于参与宿主细胞受体结合的L形尾纤维的远端部分,计算了低分辨率体积。表达并纯化了纤维的几个C端片段。获得了其中两个的晶体,它们分别属于空间群P6(3)和R32,并分别将同步加速器辐射衍射到2.3和2.9埃分辨率。还从属于空间组C2的一个片段的硒代蛋氨酸衍生的晶体中收集了设置为2.5埃分辨率的单波长异常色散数据。

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