Nature Communications (Feb 2020)
Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
- 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
Affiliations
- Joyce Woodhouse
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Gabriela Nass Kovacs
- Max-Planck-Institut für medizinische Forschung
- Nicolas Coquelle
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Lucas M. Uriarte
- Univ. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et Raman
- Virgile Adam
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Thomas R. M. Barends
- Max-Planck-Institut für medizinische Forschung
- Martin Byrdin
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Eugenio de la Mora
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- R. Bruce Doak
- Max-Planck-Institut für medizinische Forschung
- Mikolaj Feliks
- Department of Chemistry, University of Southern California
- Martin Field
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Franck Fieschi
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Virginia Guillon
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Stefan Jakobs
- Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry
- Yasumasa Joti
- Japan Synchrotron Radiation Research Institute
- Pauline Macheboeuf
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Koji Motomura
- Institute of Multidisciplinary Research for Advanced Materials, Tohoku University
- Karol Nass
- Max-Planck-Institut für medizinische Forschung
- Shigeki Owada
- RIKEN SPring-8 Center
- Christopher M. Roome
- Max-Planck-Institut für medizinische Forschung
- Cyril Ruckebusch
- Univ. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et Raman
- Giorgio Schirò
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Robert L. Shoeman
- Max-Planck-Institut für medizinische Forschung
- Michel Thepaut
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Tadashi Togashi
- Japan Synchrotron Radiation Research Institute
- Kensuke Tono
- Japan Synchrotron Radiation Research Institute
- Makina Yabashi
- RIKEN SPring-8 Center
- Marco Cammarata
- Department of Physics, UMR UR1-CNRS 6251, University of Rennes 1
- Lutz Foucar
- Max-Planck-Institut für medizinische Forschung
- Dominique Bourgeois
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Michel Sliwa
- Univ. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et Raman
- Jacques-Philippe Colletier
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- Ilme Schlichting
- Max-Planck-Institut für medizinische Forschung
- Martin Weik
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale
- DOI
- https://doi.org/10.1038/s41467-020-14537-0
- Journal volume & issue
-
Vol. 11,
no. 1
pp. 1 – 11
Abstract
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.
