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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/88972c410939421d85cfc000a74d2ee0
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Sumario: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.

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