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Membrane protein structural biology using X-ray free electron lasers

Journal article
Authors Richard Neutze
Gisela Brändén
G.F.X. Schertler
Published in Current Opinion in Structural Biology
Volume 33
Pages 115-125
ISSN 0959-440X
Publication year 2015
Published at Department of Chemistry and Molecular Biology
Pages 115-125
Language en
Links dx.doi.org/10.1016/j.sbi.2015.08.00...
Subject categories Structural Biology, Biochemistry, Molecular biophysics

Abstract

© 2015 . Membrane protein structural biology has benefitted tremendously from access to micro-focus crystallography at synchrotron radiation sources. X-ray free electron lasers (XFELs) are linear accelerator driven X-ray sources that deliver a jump in peak X-ray brilliance of nine orders of magnitude and represent a disruptive technology with potential to dramatically change the field. Membrane proteins were amongst the first macromolecules to be studied with XFEL radiation and include proof-of-principle demonstrations of serial femtosecond crystallography (SFX), the observation that XFEL data can deliver damage free crystallographic structures, initial experiments towards recording structural information from 2D arrays of membrane proteins, and time-resolved SFX, time-resolved wide angle X-ray scattering and time-resolved X-ray emission spectroscopy studies. Conversely, serial crystallography methods are now being applied using synchrotron radiation. We believe that a context dependent choice of synchrotron or XFEL radiation will accelerate progress towards novel insights in understanding membrane protein structure and dynamics.

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