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Book Chapter

Crystallographic studies of rhodopsins: structure and dynamics

MPS-Authors
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Grünbein,  Marie Luise
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Nass Kovacs,  Gabriela
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kloos,  Marco
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Gorel,  Alexander
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Doak,  R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman,  Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends,  Thomas R. M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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https://link.springer.com/protocol/10.1007/978-1-0716-2329-9_7
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https://link.springer.com/content/pdf/10.1007/978-1-0716-2329-9_7.pdf
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Citation

Grünbein, M. L., Nass Kovacs, G., Kloos, M., Gorel, A., Doak, R. B., Shoeman, R. L., et al. (2022). Crystallographic studies of rhodopsins: structure and dynamics. In Methods in Molecular Biology (pp. 147-168). New York, NY: Humana. doi:10.1007/978-1-0716-2329-9_7.


Cite as: https://hdl.handle.net/21.11116/0000-000A-C545-A
Abstract
Crystal structures have provided detailed insight in the architecture of rhodopsin photoreceptors. Of particular interest are the protein-chromophore interactions that govern the light-induced retinal isomerization and ultimately induce the large structural changes important for the various biological functions of the family. The reaction intermediates occurring along the rhodopsin photocycle have vastly differing lifetimes, from hundreds of femtoseconds to milliseconds. Detailed insight at high spatial and temporal resolution can be obtained by time-resolved crystallography using pump-probe approaches at X-ray free-electron lasers. Alternatively, cryotrapping approaches can be used. Both the approaches are described, including illumination and sample delivery. The importance of appropriate photoexcitation avoiding multiphoton absorption is stressed.