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Cryo‐EM targets in CASP14
Structures of seven CASP14 targets were determined using cryo‐electron microscopy (cryo‐EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo‐EM density maps) and experimental reference structures built into the maps....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8630773/ https://www.ncbi.nlm.nih.gov/pubmed/34398978 http://dx.doi.org/10.1002/prot.26216 |
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author | Cragnolini, Tristan Kryshtafovych, Andriy Topf, Maya |
author_facet | Cragnolini, Tristan Kryshtafovych, Andriy Topf, Maya |
author_sort | Cragnolini, Tristan |
collection | PubMed |
description | Structures of seven CASP14 targets were determined using cryo‐electron microscopy (cryo‐EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo‐EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate‐to‐density and coordinate‐to‐coordinate fit. A‐posteriori refinement of the most accurate models in their corresponding cryo‐EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less “refineable” correlate well with regions of high diversity between the CASP models and low goodness‐of‐fit to density in the reference structure. |
format | Online Article Text |
id | pubmed-8630773 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86307732022-10-14 Cryo‐EM targets in CASP14 Cragnolini, Tristan Kryshtafovych, Andriy Topf, Maya Proteins Research Articles Structures of seven CASP14 targets were determined using cryo‐electron microscopy (cryo‐EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo‐EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate‐to‐density and coordinate‐to‐coordinate fit. A‐posteriori refinement of the most accurate models in their corresponding cryo‐EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less “refineable” correlate well with regions of high diversity between the CASP models and low goodness‐of‐fit to density in the reference structure. John Wiley & Sons, Inc. 2021-09-16 2021-12 /pmc/articles/PMC8630773/ /pubmed/34398978 http://dx.doi.org/10.1002/prot.26216 Text en © 2021 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles Cragnolini, Tristan Kryshtafovych, Andriy Topf, Maya Cryo‐EM targets in CASP14 |
title |
Cryo‐EM targets in CASP14
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title_full |
Cryo‐EM targets in CASP14
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title_fullStr |
Cryo‐EM targets in CASP14
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title_full_unstemmed |
Cryo‐EM targets in CASP14
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title_short |
Cryo‐EM targets in CASP14
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title_sort | cryo‐em targets in casp14 |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8630773/ https://www.ncbi.nlm.nih.gov/pubmed/34398978 http://dx.doi.org/10.1002/prot.26216 |
work_keys_str_mv | AT cragnolinitristan cryoemtargetsincasp14 AT kryshtafovychandriy cryoemtargetsincasp14 AT topfmaya cryoemtargetsincasp14 |