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Time-Resolved Serial Femtosecond Crystallography, Towards Molecular Movies of Biomolecules in Action

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Abstract

Biological macromolecules, such as proteins, nucleic acids, and complexes thereof, are characterized by specific structural and dynamic features that are the basis of their respective biological activity, and define their dynamic personalities [29]. Understanding macromolecular activity thus requires studying structural changes over time and on various time-scales, such as equilibrium fluctuations and conformational changes orchestrating enzyme catalysis or enabling signal transduction. The first step in human vision, for instance, is the sub-picosecond time-scale photoisomerization of the retinal pigment in rhodopsin [73], which within microseconds leads to the conformational changes required for activation of transducin, the regulatory protein that initiates the signaling cascade beyond the macromolecular level.

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  1. Institute of Structural Biology, University Grenoble, Alpes, CEA, CNRS, Grenoble, France

    Jacques-Philippe Colletier, Giorgio Schirò & Martin Weik

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    Petra Fromme

  3. SLAC National Accelerator Laboratory, Menlo Park, CA, USA

    Mark S. Hunter

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Colletier, JP., Schirò, G., Weik, M. (2018). Time-Resolved Serial Femtosecond Crystallography, Towards Molecular Movies of Biomolecules in Action. In: Boutet, S., Fromme, P., Hunter, M. (eds) X-ray Free Electron Lasers. Springer, Cham. https://doi.org/10.1007/978-3-030-00551-1_11

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