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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Nature Portfolio
2020
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oai:doaj.org-article:dbd92ddaa279416f9b79929ff4e049662021-12-02T16:56:51ZSerial protein crystallography in an electron microscope10.1038/s41467-020-14793-02041-1723https://doaj.org/article/dbd92ddaa279416f9b79929ff4e049662020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14793-0https://doaj.org/toc/2041-1723For 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.Robert BückerPascal Hogan-LamarrePedram MehrabiEike C. SchulzLindsey A. BultemaYaroslav GevorkovWolfgang BrehmOleksandr YefanovDominik OberthürGünther H. KassierR. J. Dwayne MillerNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-8 (2020) |
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Science Q 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 |
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. |
format |
article |
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 |
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 Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/dbd92ddaa279416f9b79929ff4e04966 |
work_keys_str_mv |
AT robertbucker serialproteincrystallographyinanelectronmicroscope AT pascalhoganlamarre serialproteincrystallographyinanelectronmicroscope AT pedrammehrabi serialproteincrystallographyinanelectronmicroscope AT eikecschulz serialproteincrystallographyinanelectronmicroscope AT lindseyabultema serialproteincrystallographyinanelectronmicroscope AT yaroslavgevorkov serialproteincrystallographyinanelectronmicroscope AT wolfgangbrehm serialproteincrystallographyinanelectronmicroscope AT oleksandryefanov serialproteincrystallographyinanelectronmicroscope AT dominikoberthur serialproteincrystallographyinanelectronmicroscope AT guntherhkassier serialproteincrystallographyinanelectronmicroscope AT rjdwaynemiller serialproteincrystallographyinanelectronmicroscope |
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1718382710015131648 |