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Membrane protein megahertz crystallography at the European XFEL

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Veröffentlicht in: Nature Communications Vol.10.2019,1, Article number 5021, insgesamt 11 Seiten
Personen und Körperschaften: Dörner, Katerina Henrike (VerfasserIn), Wiedorn, Max Oliver (VerfasserIn), Knoska, Juraj (VerfasserIn), Gevorkov, Yaroslav (VerfasserIn), Januschek, F. (VerfasserIn), Xu, C. (VerfasserIn), Spence, John C. H. (VerfasserIn), Chapman, Henry N. (VerfasserIn), Fromme, Petra (VerfasserIn), Technische Universität Hamburg (Sonstige), Technische Universität Hamburg Vision Systems – Bildverarbeitungssysteme (Sonstige)
Titel: Membrane protein megahertz crystallography at the European XFEL/ Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere]
Format: E-Book-Kapitel
Sprache: Englisch
veröffentlicht:
2019
Gesamtaufnahme: : Nature Communications, Vol.10.2019,1, Article number 5021, insgesamt 11 Seiten
, volume:10
Quelle: Verbunddaten SWB
Lizenzfreie Online-Ressourcen
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author Dörner, Katerina Henrike, Wiedorn, Max Oliver, Knoska, Juraj, Gevorkov, Yaroslav, Januschek, F., Xu, C., Spence, John C. H., Chapman, Henry N., Fromme, Petra
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contents The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.
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spelling Dörner, Katerina Henrike VerfasserIn (DE-588)108199469X (DE-627)847412199 (DE-576)455024707 aut, Membrane protein megahertz crystallography at the European XFEL Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere], 2019, Illustrationen, Diagramme, 11, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Sonstige Körperschaft: Technische Universität Hamburg, Sonstige Körperschaft: Technische Universität Hamburg, Vision Systems – Bildverarbeitungssysteme, The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs., Wiedorn, Max Oliver VerfasserIn (DE-588)1148169202 (DE-627)1008156205 (DE-576)496274929 aut, Knoska, Juraj VerfasserIn (DE-588)1147405182 (DE-627)1006118373 (DE-576)49580021X aut, Gevorkov, Yaroslav VerfasserIn (DE-588)1184428808 (DE-627)1663544662 aut, Januschek, F. VerfasserIn (DE-588)1023326965 (DE-627)718357485 (DE-576)366649760 aut, Xu, C. VerfasserIn (DE-588)1051971527 (DE-627)787228346 (DE-576)407637117 aut, Spence, John C. H. VerfasserIn (DE-588)141845260 (DE-627)631828885 (DE-576)163138508 aut, Chapman, Henry N. 1967- VerfasserIn (DE-588)1031308059 (DE-627)736237518 (DE-576)378766325 aut, Fromme, Petra VerfasserIn (DE-588)1145627900 (DE-627)100682796X (DE-576)165709618 aut, Technische Universität Hamburg (DE-588)1112763473 (DE-627)866918418 (DE-576)476770564 oth, Technische Universität Hamburg Vision Systems – Bildverarbeitungssysteme (DE-588)118384607X (DE-627)1663370788 oth, Enthalten in Nature Communications [London] : Nature Publishing Group UK, 2010 Vol.10.2019,1, Article number 5021, insgesamt 11 Seiten Online-Ressource (DE-627)626457688 (DE-600)2553671-0 (DE-576)331555905 2041-1723 nnns, volume:10 year:2019 number:1 pages:5021 extent:11, http://nbn-resolving.de/urn:nbn:de:gbv:830-882.054954 Resolving-System kostenfrei, https://doi.org/10.15480/882.2506 Resolving-System kostenfrei, http://hdl.handle.net/11420/3790 Resolving-System kostenfrei, https://doi.org/10.1038/s41467-019-12955-3 Resolving-System, https://doi.org/10.1038/s41467-019-12955-3 LFER, http://nbn-resolving.de/urn:nbn:de:gbv:830-882.054954 LFER, LFER 2019-12-18T00:00:00Z
spellingShingle Dörner, Katerina Henrike, Wiedorn, Max Oliver, Knoska, Juraj, Gevorkov, Yaroslav, Januschek, F., Xu, C., Spence, John C. H., Chapman, Henry N., Fromme, Petra, Membrane protein megahertz crystallography at the European XFEL, The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.
title Membrane protein megahertz crystallography at the European XFEL
title_auth Membrane protein megahertz crystallography at the European XFEL
title_full Membrane protein megahertz crystallography at the European XFEL Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere]
title_fullStr Membrane protein megahertz crystallography at the European XFEL Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere]
title_full_unstemmed Membrane protein megahertz crystallography at the European XFEL Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere]
title_in_hierarchy Membrane protein megahertz crystallography at the European XFEL / Katerina Dörner, Max O. Wiedorn, Juraj Knoska, Yaroslav Gevorkov, Friederike Januschek, Chen Xu, John C. H. Spence, Henry N. Chapman, Petra Fromme [und 69 andere],
title_short Membrane protein megahertz crystallography at the European XFEL
title_sort membrane protein megahertz crystallography at the european xfel
url http://nbn-resolving.de/urn:nbn:de:gbv:830-882.054954, https://doi.org/10.15480/882.2506, http://hdl.handle.net/11420/3790, https://doi.org/10.1038/s41467-019-12955-3
urn urn:nbn:de:gbv:830-882.054954