Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy

Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy

rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resolved serial femtosecond crystallography at an X-ray...

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Autores principales: Joyce Woodhouse, Gabriela Nass Kovacs, Nicolas Coquelle, Lucas M. Uriarte, Virgile Adam, Thomas R. M. Barends, Martin Byrdin, Eugenio de la Mora, R. Bruce Doak, Mikolaj Feliks, Martin Field, Franck Fieschi, Virginia Guillon, Stefan Jakobs, Yasumasa Joti, Pauline Macheboeuf, Koji Motomura, Karol Nass, Shigeki Owada, Christopher M. Roome, Cyril Ruckebusch, Giorgio Schirò, Robert L. Shoeman, Michel Thepaut, Tadashi Togashi, Kensuke Tono, Makina Yabashi, Marco Cammarata, Lutz Foucar, Dominique Bourgeois, Michel Sliwa, Jacques-Philippe Colletier, Ilme Schlichting, Martin Weik
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/88972c410939421d85cfc000a74d2ee0
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spelling oai:doaj.org-article:88972c410939421d85cfc000a74d2ee02021-12-02T14:42:15ZPhotoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy10.1038/s41467-020-14537-02041-1723https://doaj.org/article/88972c410939421d85cfc000a74d2ee02020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14537-0https://doaj.org/toc/2041-1723rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resolved serial femtosecond crystallography at an X-ray free electron laser, and time-resolved absorption spectroscopy measurements complement their structural analysis.Joyce WoodhouseGabriela Nass KovacsNicolas CoquelleLucas M. UriarteVirgile AdamThomas R. M. BarendsMartin ByrdinEugenio de la MoraR. Bruce DoakMikolaj FeliksMartin FieldFranck FieschiVirginia GuillonStefan JakobsYasumasa JotiPauline MacheboeufKoji MotomuraKarol NassShigeki OwadaChristopher M. RoomeCyril RuckebuschGiorgio SchiròRobert L. ShoemanMichel ThepautTadashi TogashiKensuke TonoMakina YabashiMarco CammarataLutz FoucarDominique BourgeoisMichel SliwaJacques-Philippe ColletierIlme SchlichtingMartin WeikNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Joyce Woodhouse
Gabriela Nass Kovacs
Nicolas Coquelle
Lucas M. Uriarte
Virgile Adam
Thomas R. M. Barends
Martin Byrdin
Eugenio de la Mora
R. Bruce Doak
Mikolaj Feliks
Martin Field
Franck Fieschi
Virginia Guillon
Stefan Jakobs
Yasumasa Joti
Pauline Macheboeuf
Koji Motomura
Karol Nass
Shigeki Owada
Christopher M. Roome
Cyril Ruckebusch
Giorgio Schirò
Robert L. Shoeman
Michel Thepaut
Tadashi Togashi
Kensuke Tono
Makina Yabashi
Marco Cammarata
Lutz Foucar
Dominique Bourgeois
Michel Sliwa
Jacques-Philippe Colletier
Ilme Schlichting
Martin Weik
Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
description rsEGFP2 is a reversibly photoswitchable fluorescent protein used in super-resolution light microscopy. Here the authors present the structure of an rsEGFP2 ground-state intermediate after excited state-decay that was obtained by nanosecond time-resolved serial femtosecond crystallography at an X-ray free electron laser, and time-resolved absorption spectroscopy measurements complement their structural analysis.
format article
author Joyce Woodhouse
Gabriela Nass Kovacs
Nicolas Coquelle
Lucas M. Uriarte
Virgile Adam
Thomas R. M. Barends
Martin Byrdin
Eugenio de la Mora
R. Bruce Doak
Mikolaj Feliks
Martin Field
Franck Fieschi
Virginia Guillon
Stefan Jakobs
Yasumasa Joti
Pauline Macheboeuf
Koji Motomura
Karol Nass
Shigeki Owada
Christopher M. Roome
Cyril Ruckebusch
Giorgio Schirò
Robert L. Shoeman
Michel Thepaut
Tadashi Togashi
Kensuke Tono
Makina Yabashi
Marco Cammarata
Lutz Foucar
Dominique Bourgeois
Michel Sliwa
Jacques-Philippe Colletier
Ilme Schlichting
Martin Weik
author_facet Joyce Woodhouse
Gabriela Nass Kovacs
Nicolas Coquelle
Lucas M. Uriarte
Virgile Adam
Thomas R. M. Barends
Martin Byrdin
Eugenio de la Mora
R. Bruce Doak
Mikolaj Feliks
Martin Field
Franck Fieschi
Virginia Guillon
Stefan Jakobs
Yasumasa Joti
Pauline Macheboeuf
Koji Motomura
Karol Nass
Shigeki Owada
Christopher M. Roome
Cyril Ruckebusch
Giorgio Schirò
Robert L. Shoeman
Michel Thepaut
Tadashi Togashi
Kensuke Tono
Makina Yabashi
Marco Cammarata
Lutz Foucar
Dominique Bourgeois
Michel Sliwa
Jacques-Philippe Colletier
Ilme Schlichting
Martin Weik
author_sort Joyce Woodhouse
title Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
title_short Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
title_full Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
title_fullStr Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
title_full_unstemmed Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
title_sort photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/88972c410939421d85cfc000a74d2ee0
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