期刊
STRUCTURE
卷 23, 期 9, 页码 1743-1753出版社
CELL PRESS
DOI: 10.1016/j.str.2015.06.026
关键词
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资金
- FEBS
- EMBO [3-2013]
- MRC [MC_U105184326, MC_UPA0251013, MC_U105192715]
- Wellcome Trust [095514/Z/11/Z]
- European Research Council (ERC) under the European Union's Seventh Framework Programme (FP7)/ERC [261151]
- MRC [MC_U105184326, MC_UP_A025_1013, MC_U105192715] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1013, MC_U105192715, MC_U105184326] Funding Source: researchfish
Recent innovations in specimen preparation, data collection, and image processing have led to improved structure determination using single-particle electron cryomicroscopy (cryo-EM). Here we explore some of these advances to improve structures determined using electron cryotomography (cryo-ET) and sub-tomogram averaging. We implement a new three-dimensional model for the contrast transfer function, and use this in a regularized likelihood optimization algorithm as implemented in the RELION program. Using direct electron detector data, we apply both single-particle analysis and sub-tomogram averaging to analyze radiation-induced movements of the specimen. As in single-particle cryo-EM, we find that significant sample movements occur during tomographic data acquisition, and that these movements are substantially reduced through the use of ultrastable gold substrates. We obtain a sub-nanometer resolution structure of the hepatitis B capsid, and show that reducing radiation-induced specimen movement may be central to attempts at further improving tomogram quality and resolution.
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