低温电镜的分辨率记录。

Faculty reviews Pub Date : 2021-07-30 eCollection Date: 2021-01-01 DOI:10.12703/r-01-000002
Jonathan Ashmore, Bridget Carragher, Peter B Rosenthal, William Weis
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引用次数: 0

摘要

低温电子显微镜(cryoEM)是一种快速发展的结构测定技术。最近的两篇论文报道了通过平均冷冻水合生物分子的图像获得的蛋白质的第一个原子分辨率结构。他们都以前所未有的细节描述了对称的载铁蛋白组装图,这是一种常见的测试样本。两项研究中不同的新仪器改进提供了更好的图像,并且图像分析可以提取足够的结构信息来解决单个原子位置。虽然对于大多数蛋白质来说,真正的原子分辨率图还不是常规的,但研究表明,低温电子显微镜确定的结构将继续改进,增加它们在生物学和医学上的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

A resolution record for cryoEM.

A resolution record for cryoEM.

Cryo electron microscopy (cryoEM) is a fast-growing technique for structure determination. Two recent papers report the first atomic resolution structure of a protein obtained by averaging images of frozen-hydrated biomolecules. They both describe maps of symmetric apoferritin assemblies, a common test specimen, in unprecedented detail. New instrument improvements, different in the two studies, have contributed better images, and image analysis can extract structural information sufficient to resolve individual atomic positions. While true atomic resolution maps will not be routine for most proteins, the studies suggest structures determined by cryoEM will continue to improve, increasing their impact on biology and medicine.

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