Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers

Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers

X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 1012 X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish X...

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Main Author: Neutze, Richard
Format: Online
Language:English
Published: The Royal Society 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052859/
id pubmed-4052859
recordtype oai_dc
spelling pubmed-40528592014-07-17 Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers Neutze, Richard Part I: Biology X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 1012 X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish XFEL sources from synchrotron radiation. In this opinion piece, I argue that these properties of XFEL radiation will facilitate new discoveries in life science. I reason that time-resolved serial femtosecond crystallography and time-resolved wide angle X-ray scattering are promising areas of scientific investigation that will be advanced by XFEL capabilities, allowing new scientific questions to be addressed that are not accessible using established methods at storage ring facilities. These questions include visualizing ultrafast protein structural dynamics on the femtosecond to picosecond time-scale, as well as time-resolved diffraction studies of non-cyclic reactions. I argue that these emerging opportunities will stimulate a renaissance of interest in time-resolved structural biochemistry. The Royal Society 2014-07-17 /pmc/articles/PMC4052859/ /pubmed/24914150 http://dx.doi.org/10.1098/rstb.2013.0318 Text en http://creativecommons.org/licenses/by/3.0/ © 2014 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Neutze, Richard
spellingShingle Neutze, Richard
Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
author_facet Neutze, Richard
author_sort Neutze, Richard
title Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
title_short Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
title_full Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
title_fullStr Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
title_full_unstemmed Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers
title_sort opportunities and challenges for time-resolved studies of protein structural dynamics at x-ray free-electron lasers
description X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 1012 X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish XFEL sources from synchrotron radiation. In this opinion piece, I argue that these properties of XFEL radiation will facilitate new discoveries in life science. I reason that time-resolved serial femtosecond crystallography and time-resolved wide angle X-ray scattering are promising areas of scientific investigation that will be advanced by XFEL capabilities, allowing new scientific questions to be addressed that are not accessible using established methods at storage ring facilities. These questions include visualizing ultrafast protein structural dynamics on the femtosecond to picosecond time-scale, as well as time-resolved diffraction studies of non-cyclic reactions. I argue that these emerging opportunities will stimulate a renaissance of interest in time-resolved structural biochemistry.
publisher The Royal Society
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052859/
_version_ 1612099476084752384

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