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首页> 外文期刊>Crystallography reports >Expression, Purification, Crystallization and X-Ray Crystallographic Analysis of MoDabb1 from Magnaporthe oryzae
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Expression, Purification, Crystallization and X-Ray Crystallographic Analysis of MoDabb1 from Magnaporthe oryzae

机译：Modabborthe Oryzae的Modabb1的表达，纯化，结晶和X射线晶体分析

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摘要

Protein acetylation is one of the most common post-translational modifications. Many acetylated proteins in Magnaporthe oryzae play key roles in vegetative growth and pathogenicity. MoDabb1 from M. oryzae was also identified to be an acetylated protein, containing a Dabb domain with unknown function. To elucidate the function of this protein and the effect of acetylation on this protein, a native and selenomethionine-substituted MoDabb1 were expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using sitting-drop vapour-diffusion method. Crystals of native and selenomethionine-substituted protein were diffracted to a resolution of 1.74 and 1.98 angstrom and both belonged to the sp. gr. P4(2)2(1)2. Matthews coefficient analysis indicated two molecules in an asymmetric unit with a Vm value of 2.41 and a corresponding solvent content of 49.03%.
机译：蛋白质乙酰化是最常见的翻译后修饰之一。 Magnaporthe Oryzae中的许多乙酰化蛋白在营养生长和致病性中发挥关键作用。 来自M. Oryzae的Modabb1也被鉴定为乙酰化蛋白，含有具有未知功能的DABB结构域。 为了阐明该蛋白质的功能和乙酰化对该蛋白质的作用，在大肠杆菌中表达了天然和硒甲硫氨酸取代的ModaBB1并纯化为均匀性。 使用坐落蒸气扩散法获得晶体。 天然和硒甲硫氨酸取代蛋白的晶体衍生至分辨率为1.74和1.98埃，两者都属于SP。 GR。 P4（2）2（1）2。 Matthews系数分析在不对称单元中指出了两个分子，VM值为2.41，相应的溶剂含量为49.03％。

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