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Volume 122, 2003
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The frontiers of time-resolved macromolecular crystallography: movies and chirped X-ray pulses

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Abstract

Three important frontiers of ultrafast time-resolved macromolecular crystallography are presented: extension of this technique to other biological systems; further developments in the elucidation of mechanism through the analysis of time-dependent movies to extract the underlying, time-independent, intermediate structures; and enhanced time resolution. The last is intimately linked with the nature of the pump–probe experiment itself, with the sources of random and, particularly, systematic experimental error, and with the factors that contribute to overall time resolution. All experiments to date have utilized the unchirped X-ray pulses that are emitted by synchrotron sources. Chirped pulses offer certain advantages for ultrafast X-ray experiments such as those based on Laue diffraction. An energy-chirped pulse maps photon energy into time; a Laue diffraction experiment maps photon energy into detector space. Hence, a Laue experiment with an energy-chirped pulse maps time into space. The proposed sub-picosecond photon source could provide an excellent source of intense, chirped hard X-rays for such experiments.

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Publication details

The article was received on 12 Feb 2002, accepted on 19 Mar 2002 and first published on 07 Oct 2002


Article type: Paper
DOI: 10.1039/B201620F
Citation: Faraday Discuss., 2003,122, 65-77
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    The frontiers of time-resolved macromolecular crystallography: movies and chirped X-ray pulses

    K. Moffat, Faraday Discuss., 2003, 122, 65
    DOI: 10.1039/B201620F

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