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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary X-ray diffraction analysis of effector protein MoHrip2 from Magnaporthe oryzae
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Purification, crystallization and preliminary X-ray diffraction analysis of effector protein MoHrip2 from Magnaporthe oryzae

机译:稻瘟病菌效应蛋白MoHrip2的纯化,结晶及X射线初步分析

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摘要

MoHrip2, a novel effector protein from the pathogenic fungus Magnaporthe oryzae, was purified and crystallized using the sitting-drop vapour-diffusion method. Native crystals and selenomethionine-labelled crystals were obtained using 2.2 M ammonium sulfate as a precipitant. A native data set was collected to 2.0 angstrom resolution at 100 K using an in-house X-ray source and a selenomethionine-labelled data set containing anomalous signal was collected to 1.8 angstrom resolution at 100 K using a synchrotron source. Based on the anomalous signal generated from the Se atom, the MoHrip2 structure was successfully solved using the single-wavelength anomalous dispersion (SAD) method.
机译:MoHrip2是一种​​来自病原真菌米格纳霉菌的新型效应蛋白,使用坐滴蒸汽扩散法纯化和结晶。使用2.2 M硫酸铵作为沉淀剂可得到天然晶体和硒甲硫氨酸标记的晶体。使用内部X射线源在100 K下将原始数据集收集到2.0埃分辨率,并使用同步加速器源在100 K下将包含异常信号的硒代蛋氨酸标记的数据集收集到1.8埃分辨率。基于硒原子产生的异常信号,使用单波长异常色散(SAD)方法成功地解决了MoHrip2结构。

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