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首页> 外文期刊>Current Opinion in Structural Biology >Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs
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Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs

机译:低温电子显微照片的单颗粒分析确定高分子组装体的结构

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A new generation of electron microscopes equipped with field emission gun electron sources and the ability to image molecules in their native environment at liquid nitrogen or helium temperatures has enabled the analysis of macromolecular structures at medium resolution (similar to10 Angstrom) and in different conformational states. The amalgamation of electron microscopy and X-ray crystallographic approaches makes it possible to solve structures in the 100-1000 Angstrom size range, advancing our understanding of the function of complex assemblies. Many new structures have been solved during the past two years, including one of the smallest complexes to be determined by single-particle cryo-electron microscopy, the transferrin receptor-transferrin complex. Other notable results include the near atomic level resolution structure of the nicotinic acetylcholine receptor in helical arrays and an icosahedral virus structure with an asymmetric polymerase resolved.
机译:配备了场发射枪电子源的新一代电子显微镜以及在液氮或氦气温度下在其自然环境中对分子成像的能力,使得能够在中等分辨率(类似于10埃)和不同构象状态下分析大分子结构。电子显微镜和X射线晶体学方法的融合使解析100-1000埃大小范围内的结构成为可能,从而加深了我们对复杂组件功能的理解。在过去的两年中,已经解决了许多新的结构,包括通过单粒子冷冻电子显微镜确定的最小的复合物之一,即转铁蛋白受体-转铁蛋白复合物。其他显着结果包括:螺旋阵列中烟碱乙酰胆碱受体的接近原子水平的分辨结构,以及解析出不对称聚合酶的二十面体病毒结构。

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