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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
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.
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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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