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dc.contributor.authorYorke, Briony A.
dc.contributor.authorBeddard, G.S.
dc.contributor.authorOwen, R.L.
dc.contributor.authorPearson, A.R.
dc.date.accessioned2020-01-22T10:25:28Z
dc.date.available2020-01-22T10:25:28Z
dc.date.issued2014-11
dc.identifier.citationYorke BA, Beddard GS, Owen RL et al (2014) Time-resolved crystallography using the Hadamard transform. Nature Methods. 11: 1131-1134.en_US
dc.identifier.urihttp://hdl.handle.net/10454/17592
dc.descriptionYesen_US
dc.description.abstractWe describe a method for performing time-resolved X-ray crystallographic experiments based on the Hadamard transform, in which time resolution is defined by the underlying periodicity of the probe pulse sequence, and signal/noise is greatly improved over that for the fastest pump-probe experiments depending on a single pulse. This approach should be applicable on standard synchrotron beamlines and will enable high-resolution measurements of protein and small-molecule structural dynamics. It is also applicable to other time-resolved measurements where a probe can be encoded, such as pump-probe spectroscopy.en_US
dc.description.sponsorshipWellcome Trust 4-year PhD program “The Molecular Basis of Biological Mechanisms” 089312/Z/09/Z. This work was also supported by the EPSRC Award “Dynamic Structural Science at the Research Complex at Harwell” EP/I01974X/1 and by BBSRC Award BB/H001905/1.en_US
dc.language.isoenen_US
dc.rights© 2014, Springer Nature. Reproduced in accordance with the publisher's self-archiving policy. The final publication is available at https://doi.org/10.1038/nmeth.3139.en_US
dc.subjectData acquisitionen_US
dc.subjectMolecular biophysicsen_US
dc.subjectProteinsen_US
dc.subjectX-ray crystallographyen_US
dc.titleTime-resolved crystallography using the Hadamard transformen_US
dc.status.refereedYesen_US
dc.date.Accepted2014-09-04
dc.date.application2014-10-05
dc.typeArticleen_US
dc.type.versionAccepted manuscripten_US
dc.identifier.doihttps://doi.org/10.1038/nmeth.3139
refterms.dateFOA2020-01-22T10:25:56Z


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