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...
| Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2020-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-14537-0 |
| _version_ | 1818342307016998912 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-13T16:12:36Z |
| format | Article |
| id | doaj.art-88972c410939421d85cfc000a74d2ee0 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-13T16:12:36Z |
| publishDate | 2020-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-88972c410939421d85cfc000a74d2ee02022-12-21T23:38:54ZengNature PortfolioNature Communications2041-17232020-02-0111111110.1038/s41467-020-14537-0Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopyJoyce Woodhouse0Gabriela Nass Kovacs1Nicolas Coquelle2Lucas M. Uriarte3Virgile Adam4Thomas R. M. Barends5Martin Byrdin6Eugenio de la Mora7R. Bruce Doak8Mikolaj Feliks9Martin Field10Franck Fieschi11Virginia Guillon12Stefan Jakobs13Yasumasa Joti14Pauline Macheboeuf15Koji Motomura16Karol Nass17Shigeki Owada18Christopher M. Roome19Cyril Ruckebusch20Giorgio Schirò21Robert L. Shoeman22Michel Thepaut23Tadashi Togashi24Kensuke Tono25Makina Yabashi26Marco Cammarata27Lutz Foucar28Dominique Bourgeois29Michel Sliwa30Jacques-Philippe Colletier31Ilme Schlichting32Martin Weik33Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleMax-Planck-Institut für medizinische ForschungUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleUniv. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et RamanUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleMax-Planck-Institut für medizinische ForschungUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleMax-Planck-Institut für medizinische ForschungDepartment of Chemistry, University of Southern CaliforniaUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleDepartment of NanoBiophotonics, Max Planck Institute for Biophysical ChemistryJapan Synchrotron Radiation Research InstituteUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleInstitute of Multidisciplinary Research for Advanced Materials, Tohoku UniversityMax-Planck-Institut für medizinische ForschungRIKEN SPring-8 CenterMax-Planck-Institut für medizinische ForschungUniv. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et RamanUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleMax-Planck-Institut für medizinische ForschungUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleJapan Synchrotron Radiation Research InstituteJapan Synchrotron Radiation Research InstituteRIKEN SPring-8 CenterDepartment of Physics, UMR UR1-CNRS 6251, University of Rennes 1Max-Planck-Institut für medizinische ForschungUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleUniv. Lille, CNRS, UMR 8516, LASIR, Laboratoire de Spectrochimie Infrarouge et RamanUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuraleMax-Planck-Institut für medizinische ForschungUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie StructuralersEGFP2 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.https://doi.org/10.1038/s41467-020-14537-0 |
| spellingShingle | 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 Nature Communications |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41467-020-14537-0 |
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