Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.
Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.
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DOI：
10.1038/nmeth.4178
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发表时间：
2017-02-13
期刊：
影响因子：
48
通讯作者：
Gonen T
中科院分区：
文献类型：
--
作者：
de la Cruz MJ;Hattne J;Shi D;Seidler P;Rodriguez J;Reyes FE;Sawaya MR;Cascio D;Weiss SC;Kim SK;Hinck CS;Hinck AP;Calero G;Eisenberg D;Gonen T
大分子的结晶学分析依赖于大的、有序的晶体，这往往需要付出巨大的努力才能获得。即使是相当大的晶体，有时也会受到病理性的影响，使其不适合高分辨率的结构测定。在这里，我们表明，大的，不完美的晶体的碎裂可以提供一条简单的途径，通过连续的飞秒结晶学或CryoEM方法来确定高分辨率的结构。
Crystallographic analysis of macromolecules depends on large, well-ordered crystals, which often require significant effort to obtain. Even sizable crystals sometimes suffer from pathologies that render them inappropriate for high-resolution structure determination. Here we show that fragmentation of large, imperfect crystals can provide a simple path for high-resolution structure determination by serial femtosecond crystallography or the cryoEM method MicroED.