Serial protein crystallography in an electron microscope

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Veröffentlicht in:	Nature Communications Vol. 11.2020, Article number 996, insgesamt 8 Seiten
Personen und Körperschaften:	Bücker, Robert (VerfasserIn), Hogan-Lamarre, Pascal (VerfasserIn), Mehrabi, Pedram (VerfasserIn), Schulz, Eike C. (VerfasserIn), Bultema, Lindsey A. (VerfasserIn), Gevorkov, Yaroslav (VerfasserIn), Brehm, Wolfgang (VerfasserIn), Yefanov, Oleksandr (VerfasserIn), Oberthür, Dominik (VerfasserIn), Kassier, Günther H. (VerfasserIn), Miller, R. J. Dwayne (VerfasserIn), Technische Universität Hamburg (Sonstige), Technische Universität Hamburg Vision Systems – Bildverarbeitungssysteme (Sonstige)
Titel:	Serial protein crystallography in an electron microscope/ 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
Format:	E-Book-Kapitel
Sprache:	Englisch
veröffentlicht:	2020
Gesamtaufnahme:	: Nature Communications, Vol. 11.2020, Article number 996, insgesamt 8 Seiten , volume:11
Quelle:	Verbunddaten SWB Lizenzfreie Online-Ressourcen

Details
Zusammenfassung:	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 nanocrystallography. 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.
Beschreibung:	Sonstige Körperschaft: Technische Universität Hamburg Sonstige Körperschaft: Technische Universität Hamburg, Vision Systems – Bildverarbeitungssysteme
Umfang:	Illustrationen, Diagramme 8
ISSN:	2041-1723
DOI:	10.15480/882.2722