Liquid application method for time-resolved analyses by serial synchrotron 
crystallography

Mehrabi, P.; Schulz, E.-C.; Agthe, M.; Horrell, S.; Bourenkov, G.; von Stetten, D.; Leimkohl, J.-P.; Schikora, H.; Schneider, T. R.; Pearson, A. R.; Tellkamp, F.; Miller, R. J. D.

doi:10.1038/s41592-019-0553-1

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Liquid application method for time-resolved analyses by serial synchrotron crystallography

MPS-Authors

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Mehrabi, P.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Schulz, E.-C.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Centre for Ultrafast Imaging, Universität Hamburg;

/persons/resource/persons241300

Leimkohl, J.-P.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons241303

Schikora, H.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons182596

Tellkamp, F.
Machine Physics, Scientific Service Units, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

/persons/resource/persons136024

Miller, R. J. D.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Centre for Ultrafast Imaging, Universität Hamburg;
University of Toronto, Departments of Chemistry and Physics;

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https://dx.doi.org/10.1038/s41592-019-0553-1
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Citation

Mehrabi, P., Schulz, E.-C., Agthe, M., Horrell, S., Bourenkov, G., von Stetten, D., et al. (2019). Liquid application method for time-resolved analyses by serial synchrotron crystallography. Nature methods, 16(10), 979-982. doi:10.1038/s41592-019-0553-1.

Cite as: https://hdl.handle.net/21.11116/0000-0004-ADB5-D

Abstract

We introduce a liquid application method for time-resolved analyses (LAMA), an in situ mixing approach for serial crystallography. Picoliter-sized droplets are shot onto chip-mounted protein crystals, achieving near-full ligand occupancy within theoretical diffusion times. We demonstrate proof-of-principle binding of GlcNac to lysozyme, and resolve glucose binding and subsequent ring opening in a time-resolved study of xylose isomerase.