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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3
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Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3

机译:唾液腺病毒,火鸡腺病毒3的纤维蛋白C末端头部结构域的结晶

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摘要

Turkey adenovirus 3 belongs to the genus Siadenovirus. Its predicted fibre protein consists of an N-terminal virus-attachment domain, a central shaft domain and a head domain at the C-terminus. The head domain has little sequence identity to known adenovirus fibre head structures. Crystals of the fibre head domain consisting of amino acids 304-454 with an N-terminal purification tag were produced. Crystals of native and selenomethionine-derivatized protein belonged to space group I23 (unit-cell parameter 99 angstrom). They diffracted synchrotron radiation to 2.0 and 2.14 angstrom resolution, respectively, and are expected to contain one monomer in the asymmetric unit.
机译:土耳其腺病毒3属于狂犬病病毒属。其预测的纤维蛋白由C端的N端病毒附着结构域,中心轴结构域和头部结构域组成。头部结构域与已知的腺病毒纤维头部结构几乎没有序列同一性。产生了由具有N末端纯化标签的氨基酸304-454组成的纤维头部结构域的晶体。天然和硒代蛋氨酸衍生的蛋白质的晶体属于I23空间群(单位细胞参数为99埃)。他们分别将同步加速器辐射衍射到2.0和2.14埃的分辨率,并预期在不对称单元中包含一种单体。

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