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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Autores principales: 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
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/dbd92ddaa279416f9b79929ff4e04966
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spelling 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)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle 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
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AT yaroslavgevorkov serialproteincrystallographyinanelectronmicroscope
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AT dominikoberthur serialproteincrystallographyinanelectronmicroscope
AT guntherhkassier serialproteincrystallographyinanelectronmicroscope
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