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    Time-resolved crystallography using the Hadamard transform

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    Yorke_Nature_Methods (333.3Kb)
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    Publication date
    2014-11
    Author
    Yorke, Briony A.
    Beddard, G.S.
    Owen, R.L.
    Pearson, A.R.
    Keyword
    Data acquisition
    Molecular biophysics
    Proteins
    X-ray crystallography
    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.
    Peer-Reviewed
    Yes
    
    Metadata
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    Abstract
    We 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.
    URI
    http://hdl.handle.net/10454/17592
    Version
    Accepted manuscript
    Citation
    Yorke BA, Beddard GS, Owen RL et al (2014) Time-resolved crystallography using the Hadamard transform. Nature Methods. 11: 1131-1134.
    Link to publisher’s version
    https://doi.org/10.1038/nmeth.3139
    Type
    Article
    Collections
    Life Sciences Publications

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