Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography
Tomographic reconstructions of cryopreserved specimens enable in-situ structural studies. Here, the authors present the beam image-shift electron cryo-tomography (BISECT) approach that accelerates data collection speed and improves the map resolution compared to earlier approaches and present the in...
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Nature Portfolio
2021
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oai:doaj.org-article:984e7bb3da884354b7ff3bc7cde401462021-12-02T14:25:25ZBeam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography10.1038/s41467-021-22251-82041-1723https://doaj.org/article/984e7bb3da884354b7ff3bc7cde401462021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22251-8https://doaj.org/toc/2041-1723Tomographic reconstructions of cryopreserved specimens enable in-situ structural studies. Here, the authors present the beam image-shift electron cryo-tomography (BISECT) approach that accelerates data collection speed and improves the map resolution compared to earlier approaches and present the in vitro structure of a 300 kDa protein complex that was solved at 3.6 Å resolution as a test case.Jonathan BouvetteHsuan-Fu LiuXiaochen DuYe ZhouAndrew P. SikkemaJuliana da Fonseca Rezende e MelloBradley P. KlemmRick HuangRoel M. SchaaperMario J. BorgniaAlberto BartesaghiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021) |
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Science Q Jonathan Bouvette Hsuan-Fu Liu Xiaochen Du Ye Zhou Andrew P. Sikkema Juliana da Fonseca Rezende e Mello Bradley P. Klemm Rick Huang Roel M. Schaaper Mario J. Borgnia Alberto Bartesaghi Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
description |
Tomographic reconstructions of cryopreserved specimens enable in-situ structural studies. Here, the authors present the beam image-shift electron cryo-tomography (BISECT) approach that accelerates data collection speed and improves the map resolution compared to earlier approaches and present the in vitro structure of a 300 kDa protein complex that was solved at 3.6 Å resolution as a test case. |
format |
article |
author |
Jonathan Bouvette Hsuan-Fu Liu Xiaochen Du Ye Zhou Andrew P. Sikkema Juliana da Fonseca Rezende e Mello Bradley P. Klemm Rick Huang Roel M. Schaaper Mario J. Borgnia Alberto Bartesaghi |
author_facet |
Jonathan Bouvette Hsuan-Fu Liu Xiaochen Du Ye Zhou Andrew P. Sikkema Juliana da Fonseca Rezende e Mello Bradley P. Klemm Rick Huang Roel M. Schaaper Mario J. Borgnia Alberto Bartesaghi |
author_sort |
Jonathan Bouvette |
title |
Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
title_short |
Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
title_full |
Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
title_fullStr |
Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
title_full_unstemmed |
Beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
title_sort |
beam image-shift accelerated data acquisition for near-atomic resolution single-particle cryo-electron tomography |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/984e7bb3da884354b7ff3bc7cde40146 |
work_keys_str_mv |
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