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dc.contributor.author
Panneels, Valérie
dc.contributor.author
Wu, Wenting
dc.contributor.author
Tsai, Ching-Ju
dc.contributor.author
Nogly, Przemek
dc.contributor.author
Rheinberger, Jan
dc.contributor.author
Jaeger, Kathrin
dc.contributor.author
Cicchetti, Gregor
dc.contributor.author
Gati, Cornelius
dc.contributor.author
Kick, Leonhard M.
dc.contributor.author
Sala, Leonardo
dc.contributor.author
Capitani, Guido
dc.contributor.author
Milne, Chris
dc.contributor.author
Padeste, Celestino
dc.contributor.author
Pedrini, Bill
dc.contributor.author
Li, Xiao-Dan
dc.contributor.author
Standfuss, Jörg
dc.contributor.author
Abela, Rafael
dc.contributor.author
Schertler, Gebhard
dc.date.accessioned
2019-09-06T14:05:54Z
dc.date.available
2017-06-11T19:25:24Z
dc.date.available
2019-09-06T14:05:54Z
dc.date.issued
2015-07-29
dc.identifier.issn
2329-7778
dc.identifier.other
10.1063/1.4922774
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/104368
dc.identifier.doi
10.3929/ethz-b-000104368
dc.description.abstract
Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron Lasers (X-FELs) for tracking the dynamics of light-triggered processes by pump-probe serial femtosecond crystallography has been demonstrated using 3D-micron-sized crystals. In addition, X-FELs provide new opportunities for protein 2D-crystal diffraction, which would allow to observe the course of conformational changes of membrane proteins in a close-to-physiological lipid bilayer environment. Here, we describe the strategies towards structural dynamic studies of retinal proteins at room temperature, using injector or fixed-target based serial femtosecond crystallography at X-FELs. Thanks to recent progress especially in sample delivery methods, serial crystallography is now also feasible at synchrotron X-ray sources, thus expanding the possibilities for time-resolved structure determination.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
American Institute of Physics
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.title
Time-resolved structural studies with serial crystallography: A new light on retinal proteins
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 3.0 Unported
ethz.journal.title
Structural Dynamics
ethz.journal.volume
2
en_US
ethz.journal.issue
4
en_US
ethz.journal.abbreviated
Struct. Dyn.
ethz.pages.start
041718
en_US
ethz.size
8 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Melville, NY
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2017-06-11T19:26:23Z
ethz.source
ECIT
ethz.identifier.importid
imp5936537c4c8dd30432
ethz.ecitpid
pub:163345
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-15T02:48:08Z
ethz.rosetta.lastUpdated
2021-02-15T05:50:39Z
ethz.rosetta.versionExported
true
ethz.COinS
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