首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary X-ray diffraction analysis of the effector protein MoHrip1 from Magnaporthe oryzae
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Purification, crystallization and preliminary X-ray diffraction analysis of the effector protein MoHrip1 from Magnaporthe oryzae

机译:稻瘟病菌效应蛋白MoHrip1的纯化,结晶和初步X射线衍射分析

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摘要

The effector protein MoHrip1 from the pathogenic fungus Magnaporthe oryzae was purified and crystallized using the sitting-drop vapour-diffusion method. Native crystals appeared in a solution composed of 0.005 M cobalt(II) chloride hexahydrate, 0.005 M nickel(II) chloride hexahydrate, 0.005 M cadmium chloride hydrate, 0.005 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 12%(w/v) polyethylene glycol 3350. A native data set was collected to 1.9 angstrom resolution at 100 K using an in-house X-ray source. The structure of MoHrip1 was successfully determined by molecular replacement using a homologous structure.
机译:使用坐滴蒸气扩散法纯化和结晶来自病原真菌米格霉的效应蛋白MoHrip1。天然晶体出现在由0.005 M六水合氯化钴(II),0.005 M六水合氯化镍(II),0.005 M水合氯化镉,0.005 M四水合氯化镁,0.1 M HEPES pH 7.5、12%(w / v)组成的溶液中)聚乙二醇3350。使用内部X射线源在100 K下以1.9埃的分辨率收集了一个原始数据集。 MoHrip1的结构已通过使用同源结构的分子置换成功确定。

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