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Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB
Cryogenic electron microscopy (cryo-EM) methods began to be used in the mid-1970s to study thin and periodic arrays of proteins. Following a half-century of development in cryo-specimen preparation, instrumentation, data collection, data processing, and modeling software, cryo-EM has become a routin...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8050867/ https://www.ncbi.nlm.nih.gov/pubmed/33744287 http://dx.doi.org/10.1016/j.jbc.2021.100560 |
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author | Chiu, Wah Schmid, Michael F. Pintilie, Grigore D. Lawson, Catherine L. |
author_facet | Chiu, Wah Schmid, Michael F. Pintilie, Grigore D. Lawson, Catherine L. |
author_sort | Chiu, Wah |
collection | PubMed |
description | Cryogenic electron microscopy (cryo-EM) methods began to be used in the mid-1970s to study thin and periodic arrays of proteins. Following a half-century of development in cryo-specimen preparation, instrumentation, data collection, data processing, and modeling software, cryo-EM has become a routine method for solving structures from large biological assemblies to small biomolecules at near to true atomic resolution. This review explores the critical roles played by the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB) in partnership with the community to develop the necessary infrastructure to archive cryo-EM maps and associated models. Public access to cryo-EM structure data has in turn facilitated better understanding of structure–function relationships and advancement of image processing and modeling tool development. The partnership between the global cryo-EM community and PDB and EMDB leadership has synergistically shaped the standards for metadata, one-stop deposition of maps and models, and validation metrics to assess the quality of cryo-EM structures. The advent of cryo-electron tomography (cryo-ET) for in situ molecular cell structures at a broad resolution range and their correlations with other imaging data introduce new data archival challenges in terms of data size and complexity in the years to come. |
format | Online Article Text |
id | pubmed-8050867 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-80508672021-04-21 Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB Chiu, Wah Schmid, Michael F. Pintilie, Grigore D. Lawson, Catherine L. J Biol Chem JBC Reviews Cryogenic electron microscopy (cryo-EM) methods began to be used in the mid-1970s to study thin and periodic arrays of proteins. Following a half-century of development in cryo-specimen preparation, instrumentation, data collection, data processing, and modeling software, cryo-EM has become a routine method for solving structures from large biological assemblies to small biomolecules at near to true atomic resolution. This review explores the critical roles played by the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB) in partnership with the community to develop the necessary infrastructure to archive cryo-EM maps and associated models. Public access to cryo-EM structure data has in turn facilitated better understanding of structure–function relationships and advancement of image processing and modeling tool development. The partnership between the global cryo-EM community and PDB and EMDB leadership has synergistically shaped the standards for metadata, one-stop deposition of maps and models, and validation metrics to assess the quality of cryo-EM structures. The advent of cryo-electron tomography (cryo-ET) for in situ molecular cell structures at a broad resolution range and their correlations with other imaging data introduce new data archival challenges in terms of data size and complexity in the years to come. American Society for Biochemistry and Molecular Biology 2021-03-18 /pmc/articles/PMC8050867/ /pubmed/33744287 http://dx.doi.org/10.1016/j.jbc.2021.100560 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | JBC Reviews Chiu, Wah Schmid, Michael F. Pintilie, Grigore D. Lawson, Catherine L. Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title | Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title_full | Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title_fullStr | Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title_full_unstemmed | Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title_short | Evolution of standardization and dissemination of cryo-EM structures and data jointly by the community, PDB, and EMDB |
title_sort | evolution of standardization and dissemination of cryo-em structures and data jointly by the community, pdb, and emdb |
topic | JBC Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8050867/ https://www.ncbi.nlm.nih.gov/pubmed/33744287 http://dx.doi.org/10.1016/j.jbc.2021.100560 |
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