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Cryo-electron microscopy of chromatin biology
The basic unit of chromatin, the nucleosome core particle (NCP), controls how DNA in eukaryotic cells is compacted, replicated and read. Since its discovery, biochemists have sought to understand how this protein–DNA complex can help to control so many diverse tasks. Recent electron-microscopy (EM)...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458496/ https://www.ncbi.nlm.nih.gov/pubmed/28580916 http://dx.doi.org/10.1107/S2059798317004430 |
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author | Wilson, Marcus D. Costa, Alessandro |
author_facet | Wilson, Marcus D. Costa, Alessandro |
author_sort | Wilson, Marcus D. |
collection | PubMed |
description | The basic unit of chromatin, the nucleosome core particle (NCP), controls how DNA in eukaryotic cells is compacted, replicated and read. Since its discovery, biochemists have sought to understand how this protein–DNA complex can help to control so many diverse tasks. Recent electron-microscopy (EM) studies on NCP-containing assemblies have helped to describe important chromatin transactions at a molecular level. With the implementation of recent technical advances in single-particle EM, our understanding of how nucleosomes are recognized and read looks to take a leap forward. In this review, the authors highlight recent advances in the architectural understanding of chromatin biology elucidated by EM. |
format | Online Article Text |
id | pubmed-5458496 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-54584962017-06-27 Cryo-electron microscopy of chromatin biology Wilson, Marcus D. Costa, Alessandro Acta Crystallogr D Struct Biol Research Papers The basic unit of chromatin, the nucleosome core particle (NCP), controls how DNA in eukaryotic cells is compacted, replicated and read. Since its discovery, biochemists have sought to understand how this protein–DNA complex can help to control so many diverse tasks. Recent electron-microscopy (EM) studies on NCP-containing assemblies have helped to describe important chromatin transactions at a molecular level. With the implementation of recent technical advances in single-particle EM, our understanding of how nucleosomes are recognized and read looks to take a leap forward. In this review, the authors highlight recent advances in the architectural understanding of chromatin biology elucidated by EM. International Union of Crystallography 2017-04-20 /pmc/articles/PMC5458496/ /pubmed/28580916 http://dx.doi.org/10.1107/S2059798317004430 Text en © Wilson & Costa 2017 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Papers Wilson, Marcus D. Costa, Alessandro Cryo-electron microscopy of chromatin biology |
title | Cryo-electron microscopy of chromatin biology |
title_full | Cryo-electron microscopy of chromatin biology |
title_fullStr | Cryo-electron microscopy of chromatin biology |
title_full_unstemmed | Cryo-electron microscopy of chromatin biology |
title_short | Cryo-electron microscopy of chromatin biology |
title_sort | cryo-electron microscopy of chromatin biology |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5458496/ https://www.ncbi.nlm.nih.gov/pubmed/28580916 http://dx.doi.org/10.1107/S2059798317004430 |
work_keys_str_mv | AT wilsonmarcusd cryoelectronmicroscopyofchromatinbiology AT costaalessandro cryoelectronmicroscopyofchromatinbiology |