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Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals
Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. I...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6327180/ https://www.ncbi.nlm.nih.gov/pubmed/30713701 http://dx.doi.org/10.1107/S2052252518014641 |
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author | Casadei, Cecilia M. Nass, Karol Barty, Anton Hunter, Mark S. Padeste, Celestino Tsai, Ching-Ju Boutet, Sébastien Messerschmidt, Marc Sala, Leonardo Williams, Garth J. Ozerov, Dmitry Coleman, Matthew Li, Xiao-Dan Frank, Matthias Pedrini, Bill |
author_facet | Casadei, Cecilia M. Nass, Karol Barty, Anton Hunter, Mark S. Padeste, Celestino Tsai, Ching-Ju Boutet, Sébastien Messerschmidt, Marc Sala, Leonardo Williams, Garth J. Ozerov, Dmitry Coleman, Matthew Li, Xiao-Dan Frank, Matthias Pedrini, Bill |
author_sort | Casadei, Cecilia M. |
collection | PubMed |
description | Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments. |
format | Online Article Text |
id | pubmed-6327180 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-63271802019-02-01 Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals Casadei, Cecilia M. Nass, Karol Barty, Anton Hunter, Mark S. Padeste, Celestino Tsai, Ching-Ju Boutet, Sébastien Messerschmidt, Marc Sala, Leonardo Williams, Garth J. Ozerov, Dmitry Coleman, Matthew Li, Xiao-Dan Frank, Matthias Pedrini, Bill IUCrJ Research Papers Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments. International Union of Crystallography 2019-01-01 /pmc/articles/PMC6327180/ /pubmed/30713701 http://dx.doi.org/10.1107/S2052252518014641 Text en © Casadei et al. 2019 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 Casadei, Cecilia M. Nass, Karol Barty, Anton Hunter, Mark S. Padeste, Celestino Tsai, Ching-Ju Boutet, Sébastien Messerschmidt, Marc Sala, Leonardo Williams, Garth J. Ozerov, Dmitry Coleman, Matthew Li, Xiao-Dan Frank, Matthias Pedrini, Bill Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title | Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title_full | Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title_fullStr | Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title_full_unstemmed | Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title_short | Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
title_sort | structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6327180/ https://www.ncbi.nlm.nih.gov/pubmed/30713701 http://dx.doi.org/10.1107/S2052252518014641 |
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