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TitleSerial protein crystallography in an electron microscope.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 996, Year 2020
Publish dateFeb 21, 2020
AuthorsRobert 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 /
PubMed AbstractSerial 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 ...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.
External linksNat Commun / PubMed:32081905 / PubMed Central
MethodsEM (electron crystallography)
Resolution1.6 - 1.8 Å
Structure data

10090

6s2n

EMDB-10090, PDB-6s2n:
Hen egg-white lysozyme by serial electron diffraction
Method: EM (electron crystallography) / Resolution: 1.8 Å

10091

6s2o

EMDB-10091, PDB-6s2o:
Granulovirus occlusion bodies by serial electron diffraction
Method: EM (electron crystallography) / Resolution: 1.6 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • gallus gallus (chicken)
  • Chicken (chicken)
  • cydia pomonella granulosis virus (isolate mexico/1963)
KeywordsHYDROLASE / lysozyme / HEWL / serial crystallography / VIRAL PROTEIN / granulovirus / occlusion body

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