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Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals

There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part...

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Autores principales: Uervirojnangkoorn, Monarin, Zeldin, Oliver B, Lyubimov, Artem Y, Hattne, Johan, Brewster, Aaron S, Sauter, Nicholas K, Brunger, Axel T, Weis, William I
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4397907/
https://www.ncbi.nlm.nih.gov/pubmed/25781634
http://dx.doi.org/10.7554/eLife.05421
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author Uervirojnangkoorn, Monarin
Zeldin, Oliver B
Lyubimov, Artem Y
Hattne, Johan
Brewster, Aaron S
Sauter, Nicholas K
Brunger, Axel T
Weis, William I
author_facet Uervirojnangkoorn, Monarin
Zeldin, Oliver B
Lyubimov, Artem Y
Hattne, Johan
Brewster, Aaron S
Sauter, Nicholas K
Brunger, Axel T
Weis, William I
author_sort Uervirojnangkoorn, Monarin
collection PubMed
description There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited. DOI: http://dx.doi.org/10.7554/eLife.05421.001
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spelling pubmed-43979072015-04-17 Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals Uervirojnangkoorn, Monarin Zeldin, Oliver B Lyubimov, Artem Y Hattne, Johan Brewster, Aaron S Sauter, Nicholas K Brunger, Axel T Weis, William I eLife Biophysics and Structural Biology There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited. DOI: http://dx.doi.org/10.7554/eLife.05421.001 eLife Sciences Publications, Ltd 2015-03-17 /pmc/articles/PMC4397907/ /pubmed/25781634 http://dx.doi.org/10.7554/eLife.05421 Text en http://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication (http://creativecommons.org/publicdomain/zero/1.0/) .
spellingShingle Biophysics and Structural Biology
Uervirojnangkoorn, Monarin
Zeldin, Oliver B
Lyubimov, Artem Y
Hattne, Johan
Brewster, Aaron S
Sauter, Nicholas K
Brunger, Axel T
Weis, William I
Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title_full Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title_fullStr Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title_full_unstemmed Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title_short Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
title_sort enabling x-ray free electron laser crystallography for challenging biological systems from a limited number of crystals
topic Biophysics and Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4397907/
https://www.ncbi.nlm.nih.gov/pubmed/25781634
http://dx.doi.org/10.7554/eLife.05421
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