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  Serial protein crystallography in an electron microscope

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-AC09-0 Version Permalink: https://hdl.handle.net/21.11116/0000-0006-06BC-0
Genre: Journal Article

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 Creators:
Bücker, R.1, 2, Author           
Hogan-Lamarre, P.1, 2, 3, Author           
Mehrabi, P.1, 2, Author           
Schulz, E.-C.1, 2, Author           
Bultema, L.1, 2, Author           
Gevorkov, Y.4, 5, Author
Brehm, W.4, Author
Yefanov, O.4, Author
Oberthür, D.4, Author
Kassier, G.1, 2, Author           
Miller, R. J. D.1, 2, 3, Author           
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Center for Free-Electron Laser Science, ou_persistent22              
3Departments of Chemistry and Physics, University of Toronto, ou_persistent22              
4Center for Free-Electron Laser Science, DESY, ou_persistent22              
5Institute of Vision Systems, Hamburg University of Technology, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2019-11-122020-01-272020-02-21
 Publication Status: Published online
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-020-14793-0
 Degree: -

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Project name : We thank Djordje Gitaric for mechanical design work, Fabian Westermeier, David Pennicard, and Heinz Graafsma for adapting the Lambda detector for electron imaging, Anton Barty and Henry Chapman for many helpful discussions and critical reading of the manuscript, Thomas A. White for help with modifying CrystFEL for electron diffraction, and Michiel de Kock for help with image processing. We are indebted to Kay Grünewald and his research group for lending to us their cryo-transfer holder. We gratefully acknowledge the support provided by the Max Planck Society, Deutsches Elektronen-Synchrotron (DESY), the excellence cluster “The Hamburg Center for Ultrafast Imaging” of the Deutsche Forschungsgemeinschaft (EXC 1074 project ID 194651731), the European Research Council project “Attosecond X-ray Science: Imaging and Spectroscopy” (Award/Contract Number ERC-2013-SyG 609920), and the Joachim Herz Foundation (Biomedical Physics of Infection). P.H. acknowledges support by the Natural Sciences and Engineering Research Council of Canada. P.M. was supported by the Alexander von Humboldt-Stiftung for postdoctoral researchers.
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 (1) Sequence Number: 996 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723