首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray crystallographic analysis of a helicase-like domain from a tomato mosaic virus replication protein
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Crystallization and preliminary X-ray crystallographic analysis of a helicase-like domain from a tomato mosaic virus replication protein

机译:番茄花叶病毒复制蛋白中解旋酶样结构域的结晶和初步X射线晶体学分析

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摘要

Tomato mosaic virus belongs to the genus Tobamovirus in the alphavirus-like superfamily of positive-strand RNA viruses. The alphavirus-like superfamily includes many plant and animal viruses of agronomical and clinical importance. These viruses encode replication-associated proteins that contain a putative superfamily 1 helicase domain. No three-dimensional structures for this domain have been determined to date. Here, the crystallization and preliminary X-ray diffraction analysis of the 130K helicase domain are reported. Diffraction data were collected and processed to 2.05 and 1.75 Å resolution from native and selenomethionine-labelled crystals, respectively. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 85.8, b = 128.3, c = 40.7 Å.
机译:番茄花叶病毒属于正链RNA病毒的类似alphavirus的超家族中的Tobamovirus属。类似甲病毒的超家族包括许多具有农学和临床重要性的动植物病毒。这些病毒编码包含推定的超家族1解旋酶结构域的复制相关蛋白。迄今为止,尚未确定此领域的三维结构。在此,报道了130K解旋酶结构域的结晶和初步X射线衍射分析。收集衍射数据,并分别从天然和硒代蛋氨酸标记的晶体中将其加工成2.05和1.75Å的分辨率。晶体属于正交晶空间群P212121,晶胞参数a = 85.8,b = 128.3,c = 40.7。

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