Serial protein crystallography in an electron microscope
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Serial protein crystallography in an electron microscope. / Bücker, Robert; Hogan-Lamarre, Pascal; Mehrabi, Pedram; Schulz, Eike C; Bultema, Lindsey A; Gevorkov, Yaroslav; Brehm, Wolfgang; Yefanov, Oleksandr; Oberthür, Dominik; Kassier, Günther H; Dwayne Miller, R J.
in: NAT COMMUN, Jahrgang 11, Nr. 1, 996, 21.02.2020.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Serial protein crystallography in an electron microscope
AU - Bücker, Robert
AU - Hogan-Lamarre, Pascal
AU - Mehrabi, Pedram
AU - Schulz, Eike C
AU - Bultema, Lindsey A
AU - Gevorkov, Yaroslav
AU - Brehm, Wolfgang
AU - Yefanov, Oleksandr
AU - Oberthür, Dominik
AU - Kassier, Günther H
AU - Dwayne Miller, R J
PY - 2020/2/21
Y1 - 2020/2/21
N2 - 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.
AB - 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.
KW - Crystallography/methods
KW - Microscopy, Electron, Scanning Transmission
KW - Models, Molecular
KW - Muramidase/chemistry
KW - Nanoparticles/chemistry
KW - Occlusion Body Matrix Proteins/chemistry
KW - Particle Size
KW - Protein Conformation
KW - Proteins/chemistry
U2 - 10.1038/s41467-020-14793-0
DO - 10.1038/s41467-020-14793-0
M3 - SCORING: Journal article
C2 - 32081905
VL - 11
JO - NAT COMMUN
JF - NAT COMMUN
SN - 2041-1723
IS - 1
M1 - 996
ER -
