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Integral membrane proteins and free electron lasers – a compatible couple indeed!
Several structures of membrane transport proteins in complex with mechanistically-relevant ligands, determined by serial femtosecond crystallography of microcrystals at an X-ray free-electron source source, are presented. These results, including investigation of approaches to data quality assessmen...
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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International Union of Crystallography
2015
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4491310/ https://www.ncbi.nlm.nih.gov/pubmed/26175898 http://dx.doi.org/10.1107/S2052252515012294 |
| _version_ | 1782379619550232576 |
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| author | Wiener, Michael C. |
| author_facet | Wiener, Michael C. |
| author_sort | Wiener, Michael C. |
| collection | PubMed |
| description | Several structures of membrane transport proteins in complex with mechanistically-relevant ligands, determined by serial femtosecond crystallography of microcrystals at an X-ray free-electron source source, are presented. These results, including investigation of approaches to data quality assessment and refinement from low-redundancy data, indicate the feasibility of using this approach for ligand screening. |
| format | Online Article Text |
| id | pubmed-4491310 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2015 |
| publisher | International Union of Crystallography |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-44913102015-07-14 Integral membrane proteins and free electron lasers – a compatible couple indeed! Wiener, Michael C. IUCrJ Scientific Commentaries Several structures of membrane transport proteins in complex with mechanistically-relevant ligands, determined by serial femtosecond crystallography of microcrystals at an X-ray free-electron source source, are presented. These results, including investigation of approaches to data quality assessment and refinement from low-redundancy data, indicate the feasibility of using this approach for ligand screening. International Union of Crystallography 2015-06-30 /pmc/articles/PMC4491310/ /pubmed/26175898 http://dx.doi.org/10.1107/S2052252515012294 Text en © Michael C. Wiener 2015 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 | Scientific Commentaries Wiener, Michael C. Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title | Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title_full | Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title_fullStr | Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title_full_unstemmed | Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title_short | Integral membrane proteins and free electron lasers – a compatible couple indeed! |
| title_sort | integral membrane proteins and free electron lasers – a compatible couple indeed! |
| topic | Scientific Commentaries |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4491310/ https://www.ncbi.nlm.nih.gov/pubmed/26175898 http://dx.doi.org/10.1107/S2052252515012294 |
| work_keys_str_mv | AT wienermichaelc integralmembraneproteinsandfreeelectronlasersacompatiblecoupleindeed |