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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....

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Detalles Bibliográficos
Autores principales: Cragnolini, Tristan, Kryshtafovych, Andriy, Topf, Maya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2021
Materias:
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.
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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
title_full Cryo‐EM targets in CASP14
title_fullStr Cryo‐EM targets in CASP14
title_full_unstemmed Cryo‐EM targets in CASP14
title_short Cryo‐EM targets in CASP14
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
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