Cargando…
Automating crystallographic structure solution and refinement of protein–ligand complexes
High-throughput drug-discovery and mechanistic studies often require the determination of multiple related crystal structures that only differ in the bound ligands, point mutations in the protein sequence and minor conformational changes. If performed manually, solution and refinement requires exten...
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919266/ https://www.ncbi.nlm.nih.gov/pubmed/24419387 http://dx.doi.org/10.1107/S139900471302748X |
_version_ | 1782303038910758912 |
---|---|
author | Echols, Nathaniel Moriarty, Nigel W. Klei, Herbert E. Afonine, Pavel V. Bunkóczi, Gábor Headd, Jeffrey J. McCoy, Airlie J. Oeffner, Robert D. Read, Randy J. Terwilliger, Thomas C. Adams, Paul D. |
author_facet | Echols, Nathaniel Moriarty, Nigel W. Klei, Herbert E. Afonine, Pavel V. Bunkóczi, Gábor Headd, Jeffrey J. McCoy, Airlie J. Oeffner, Robert D. Read, Randy J. Terwilliger, Thomas C. Adams, Paul D. |
author_sort | Echols, Nathaniel |
collection | PubMed |
description | High-throughput drug-discovery and mechanistic studies often require the determination of multiple related crystal structures that only differ in the bound ligands, point mutations in the protein sequence and minor conformational changes. If performed manually, solution and refinement requires extensive repetition of the same tasks for each structure. To accelerate this process and minimize manual effort, a pipeline encompassing all stages of ligand building and refinement, starting from integrated and scaled diffraction intensities, has been implemented in Phenix. The resulting system is able to successfully solve and refine large collections of structures in parallel without extensive user intervention prior to the final stages of model completion and validation. |
format | Online Article Text |
id | pubmed-3919266 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-39192662014-02-13 Automating crystallographic structure solution and refinement of protein–ligand complexes Echols, Nathaniel Moriarty, Nigel W. Klei, Herbert E. Afonine, Pavel V. Bunkóczi, Gábor Headd, Jeffrey J. McCoy, Airlie J. Oeffner, Robert D. Read, Randy J. Terwilliger, Thomas C. Adams, Paul D. Acta Crystallogr D Biol Crystallogr Research Papers High-throughput drug-discovery and mechanistic studies often require the determination of multiple related crystal structures that only differ in the bound ligands, point mutations in the protein sequence and minor conformational changes. If performed manually, solution and refinement requires extensive repetition of the same tasks for each structure. To accelerate this process and minimize manual effort, a pipeline encompassing all stages of ligand building and refinement, starting from integrated and scaled diffraction intensities, has been implemented in Phenix. The resulting system is able to successfully solve and refine large collections of structures in parallel without extensive user intervention prior to the final stages of model completion and validation. International Union of Crystallography 2013-12-25 /pmc/articles/PMC3919266/ /pubmed/24419387 http://dx.doi.org/10.1107/S139900471302748X Text en © Echols et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Papers Echols, Nathaniel Moriarty, Nigel W. Klei, Herbert E. Afonine, Pavel V. Bunkóczi, Gábor Headd, Jeffrey J. McCoy, Airlie J. Oeffner, Robert D. Read, Randy J. Terwilliger, Thomas C. Adams, Paul D. Automating crystallographic structure solution and refinement of protein–ligand complexes |
title | Automating crystallographic structure solution and refinement of protein–ligand complexes |
title_full | Automating crystallographic structure solution and refinement of protein–ligand complexes |
title_fullStr | Automating crystallographic structure solution and refinement of protein–ligand complexes |
title_full_unstemmed | Automating crystallographic structure solution and refinement of protein–ligand complexes |
title_short | Automating crystallographic structure solution and refinement of protein–ligand complexes |
title_sort | automating crystallographic structure solution and refinement of protein–ligand complexes |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3919266/ https://www.ncbi.nlm.nih.gov/pubmed/24419387 http://dx.doi.org/10.1107/S139900471302748X |
work_keys_str_mv | AT echolsnathaniel automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT moriartynigelw automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT kleiherberte automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT afoninepavelv automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT bunkoczigabor automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT headdjeffreyj automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT mccoyairliej automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT oeffnerrobertd automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT readrandyj automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT terwilligerthomasc automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes AT adamspauld automatingcrystallographicstructuresolutionandrefinementofproteinligandcomplexes |