Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals
Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals
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DOI：
10.1016/j.jsb.2012.04.025
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发表时间：
2012-10-01
影响因子：
3
通讯作者：
Glaeser, Robert M.
中科院分区：
文献类型：
--
作者：
Han, Bong-Gyoon;Walton, Ross W.;Glaeser, Robert M.
蛋白质复合物的化学生物素化，然后结合到二维（单层）链霉亲和素晶体被证明是一种有效的方法，从低蛋白质浓度的样品中制备低温电镜样品。三种不同的多蛋白复合物被用来证明这种方法的普遍性。此外，使用从Sulfolobus solfataricus P2中纯化的天然热体来证明产生均匀分布的欧拉角，即使已知该颗粒在使用其他冷冻电镜样品制备方法时采用首选取向。(C) 2012爱思唯尔公司版权所有。
Chemical biotinylation of protein complexes followed by binding to two-dimensional (monolayer) crystals of streptavidin is shown to be an effective way to prepare cryo-EM specimens from samples at low protein concentration. Three different multiprotein complexes are used to demonstrate the generality of this method. In addition, native thermosomes, purified from Sulfolobus solfataricus P2, are used to demonstrate that a uniform distribution of Euler angles is produced, even though this particle is known to adopt a preferred orientation when other methods of cryo-EM specimen preparation are used. (C) 2012 Elsevier Inc. All rights reserved.