Serial protein crystallography in an electron microscope
For conventional three-dimensional microcrystal electron diffraction (3D ED/MicroED), a crystal is slowly rotated under an electron beam, leading to inevitable accumulation of radiation damage during data collection. In this work, the authors present a serial electron diffraction method, where still...
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| Language: | English |
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Nature Publishing Group
2020-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-14793-0 |
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doaj-dbd92ddaa279416f9b79929ff4e049662021-05-11T09:00:10ZengNature Publishing GroupNature Communications2041-17232020-02-011111810.1038/s41467-020-14793-0Serial protein crystallography in an electron microscopeRobert Bücker0Pascal Hogan-Lamarre1Pedram Mehrabi2Eike C. Schulz3Lindsey A. Bultema4Yaroslav Gevorkov5Wolfgang Brehm6Oleksandr Yefanov7Dominik Oberthür8Günther H. Kassier9R. J. Dwayne Miller10Max Planck Institute for the Structure and Dynamics of Matter, CFELMax Planck Institute for the Structure and Dynamics of Matter, CFELMax Planck Institute for the Structure and Dynamics of Matter, CFELMax Planck Institute for the Structure and Dynamics of Matter, CFELMax Planck Institute for the Structure and Dynamics of Matter, CFELCenter for Free-Electron Laser Science, DESYCenter for Free-Electron Laser Science, DESYCenter for Free-Electron Laser Science, DESYCenter for Free-Electron Laser Science, DESYMax Planck Institute for the Structure and Dynamics of Matter, CFELMax Planck Institute for the Structure and Dynamics of Matter, CFELFor conventional three-dimensional microcrystal electron diffraction (3D ED/MicroED), a crystal is slowly rotated under an electron beam, leading to inevitable accumulation of radiation damage during data collection. In this work, the authors present a serial electron diffraction method, where still diffraction patterns from many protein nanocrystals are rapidly recorded and merged, which minimises radiation damage and only requires a slightly modified standard scanning transmission electron microscope.https://doi.org/10.1038/s41467-020-14793-0 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Robert Bücker Pascal Hogan-Lamarre Pedram Mehrabi Eike C. Schulz Lindsey A. Bultema Yaroslav Gevorkov Wolfgang Brehm Oleksandr Yefanov Dominik Oberthür Günther H. Kassier R. J. Dwayne Miller |
| spellingShingle |
Robert Bücker Pascal Hogan-Lamarre Pedram Mehrabi Eike C. Schulz Lindsey A. Bultema Yaroslav Gevorkov Wolfgang Brehm Oleksandr Yefanov Dominik Oberthür Günther H. Kassier R. J. Dwayne Miller Serial protein crystallography in an electron microscope Nature Communications |
| author_facet |
Robert Bücker Pascal Hogan-Lamarre Pedram Mehrabi Eike C. Schulz Lindsey A. Bultema Yaroslav Gevorkov Wolfgang Brehm Oleksandr Yefanov Dominik Oberthür Günther H. Kassier R. J. Dwayne Miller |
| author_sort |
Robert Bücker |
| title |
Serial protein crystallography in an electron microscope |
| title_short |
Serial protein crystallography in an electron microscope |
| title_full |
Serial protein crystallography in an electron microscope |
| title_fullStr |
Serial protein crystallography in an electron microscope |
| title_full_unstemmed |
Serial protein crystallography in an electron microscope |
| title_sort |
serial protein crystallography in an electron microscope |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2020-02-01 |
| description |
For conventional three-dimensional microcrystal electron diffraction (3D ED/MicroED), a crystal is slowly rotated under an electron beam, leading to inevitable accumulation of radiation damage during data collection. In this work, the authors present a serial electron diffraction method, where still diffraction patterns from many protein nanocrystals are rapidly recorded and merged, which minimises radiation damage and only requires a slightly modified standard scanning transmission electron microscope. |
| url |
https://doi.org/10.1038/s41467-020-14793-0 |
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