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

Authors :
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 SchirĂ²
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
Source :
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Publication Year :
2020
Publisher :
Nature Portfolio, 2020.

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.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
11
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.88972c410939421d85cfc000a74d2ee0
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-020-14537-0