Serial protein crystallography in an electron microscope

Bücker, R.; Hogan-Lamarre, P.; Mehrabi, P.; Schulz, E. C.; Bultema, L.; Gevorkov, Y.; Brehm, W.; Yefanov, O.; Oberthür, D.; Kassier, G. H.; Miller, R. J. D.

doi:10.1038/s41467-020-14793-0

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Serial protein crystallography in an electron microscope

MPS-Authors

Bücker, R.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;

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Hogan-Lamarre, P.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;
International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Departments of Chemistry and Physics, University of Toronto;

Mehrabi, P.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;

Schulz, E. C.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;

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Bultema, L.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;
International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

Kassier, G. H.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;

Miller, R. J. D.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Center for Free-Electron Laser Science;
Departments of Chemistry and Physics, University of Toronto;

External Resource

https://dx.doi.org/doi.org/10.1101/682575
(Preprint)

https://dx.doi.org/10.1038/s41467-020-14793-0
(Publisher version)

https://www.nature.com/articles/s41467-020-14793-0#Sec13
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s41467-020-14793-0.pdf
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Citation

Bücker, R., Hogan-Lamarre, P., Mehrabi, P., Schulz, E. C., Bultema, L., Gevorkov, Y., et al. (2020). Serial protein crystallography in an electron microscope. Nature Communications, 11(1): 996. doi:10.1038/s41467-020-14793-0.

Cite as: https://hdl.handle.net/21.11116/0000-0005-D9F8-F

Abstract

Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from sub-micron-sized crystals. However, beam time at these facilities is scarce, and involved sample delivery techniques are required. On the other hand, rotation electron diffraction (MicroED) has shown great potential as an alternative means for protein nano-crystallography. Here, we present a method for serial electron diffraction of protein nanocrystals combining the benefits of both approaches. In a scanning transmission electron microscope, crystals randomly dispersed on a sample grid are automatically mapped, and a diffraction pattern at fixed orientation is recorded from each at a high acquisition rate. Dose fractionation ensures minimal radiation damage effects. We demonstrate the method by solving the structure of granulovirus occlusion bodies and lysozyme to resolutions of 1.55 Å and 1.80 Å, respectively. Our method promises to provide rapid structure determination for many classes of materials with minimal sample consumption, using readily available instrumentation.