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Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV
Nearly 98% of single particle cryo-EM structures resolved to better than 4 Å resolution have been determined using 300 keV transmission electron microscopes. We demonstrate that it is possible to obtain reconstructions of macromolecular complexes at a range of sizes to better than 3 Å resolution usi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5679434/ https://www.ncbi.nlm.nih.gov/pubmed/28991891 http://dx.doi.org/10.1038/nmeth.4461 |
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author | Herzik, Mark A. Wu, Mengyu Lander, Gabriel C. |
author_facet | Herzik, Mark A. Wu, Mengyu Lander, Gabriel C. |
author_sort | Herzik, Mark A. |
collection | PubMed |
description | Nearly 98% of single particle cryo-EM structures resolved to better than 4 Å resolution have been determined using 300 keV transmission electron microscopes. We demonstrate that it is possible to obtain reconstructions of macromolecular complexes at a range of sizes to better than 3 Å resolution using a 200 keV transmission electron microscope. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules. |
format | Online Article Text |
id | pubmed-5679434 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
record_format | MEDLINE/PubMed |
spelling | pubmed-56794342018-04-09 Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV Herzik, Mark A. Wu, Mengyu Lander, Gabriel C. Nat Methods Article Nearly 98% of single particle cryo-EM structures resolved to better than 4 Å resolution have been determined using 300 keV transmission electron microscopes. We demonstrate that it is possible to obtain reconstructions of macromolecular complexes at a range of sizes to better than 3 Å resolution using a 200 keV transmission electron microscope. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules. 2017-10-09 2017-11 /pmc/articles/PMC5679434/ /pubmed/28991891 http://dx.doi.org/10.1038/nmeth.4461 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Herzik, Mark A. Wu, Mengyu Lander, Gabriel C. Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title | Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title_full | Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title_fullStr | Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title_full_unstemmed | Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title_short | Achieving better than 3 Å resolution by single particle cryo-EM at 200 keV |
title_sort | achieving better than 3 å resolution by single particle cryo-em at 200 kev |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5679434/ https://www.ncbi.nlm.nih.gov/pubmed/28991891 http://dx.doi.org/10.1038/nmeth.4461 |
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