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The room temperature crystal structure of a bacterial phytochrome determined by serial femtosecond crystallography

Journal article
Authors Petra Edlund
Heikki Takala
Elin Claesson
Léocadie Henry
Robert Dods
Heli Lehtivuori
Matthijs R Panman
K. Pande
T. White
T. Nakane
Oskar Berntsson
Emil Gustavsson
Petra Båth
V. Modi
S. Roy-Chowdhury
J. Zook
P. Berntsen
S. Pandey
I. Poudyal
J. Tenboer
C. Kupitz
A. Barty
P. Fromme
J. D. Koralek
T. Tanaka
J. Spence
M. L. Liang
M. S. Hunter
S. Boutet
E. Nango
K. Moffat
G. Groenhof
J. Ihalainen
E. A. Stojkovic
M. Schmidt
Sebastian Westenhoff
Published in Scientific Reports
Volume 6
ISSN 2045-2322
Publication year 2016
Published at Department of Chemistry and Molecular Biology
Language en
Subject categories Chemical Sciences, Structural Biology


Phytochromes are a family of photoreceptors that control light responses of plants, fungi and bacteria. A sequence of structural changes, which is not yet fully understood, leads to activation of an output domain. Time-resolved serial femtosecond crystallography (SFX) can potentially shine light on these conformational changes. Here we report the room temperature crystal structure of the chromophore-binding domains of the Deinococcus radiodurans phytochrome at 2.1 angstrom resolution. The structure was obtained by serial femtosecond X-ray crystallography from microcrystals at an X-ray free electron laser. We find overall good agreement compared to a crystal structure at 1.35 angstrom resolution derived from conventional crystallography at cryogenic temperatures, which we also report here. The thioether linkage between chromophore and protein is subject to positional ambiguity at the synchrotron, but is fully resolved with SFX. The study paves the way for time-resolved structural investigations of the phytochrome photocycle with time-resolved SFX.

Page Manager: Webmaster|Last update: 9/11/2012

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