000435853 001__ 435853 000435853 005__ 20250729150119.0 000435853 0247_ $$2doi$$a10.1038/s41467-020-14793-0 000435853 0247_ $$2datacite_doi$$a10.3204/PUBDB-2020-00822 000435853 0247_ $$2altmetric$$aaltmetric:76444364 000435853 0247_ $$2pmid$$apmid:32081905 000435853 0247_ $$2WOS$$aWOS:000517991000002 000435853 0247_ $$2openalex$$aopenalex:W3006974456 000435853 037__ $$aPUBDB-2020-00822 000435853 041__ $$aEnglish 000435853 082__ $$a500 000435853 1001_ $$00000-0001-7654-4707$$aBücker, Robert$$b0 000435853 245__ $$aSerial protein crystallography in an electron microscope 000435853 260__ $$a[London]$$bNature Publishing Group UK$$c2020 000435853 3367_ $$2DRIVER$$aarticle 000435853 3367_ $$2DataCite$$aOutput Types/Journal article 000435853 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1718100653_2862555 000435853 3367_ $$2BibTeX$$aARTICLE 000435853 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000435853 3367_ $$00$$2EndNote$$aJournal Article 000435853 500__ $$aopen access 000435853 520__ $$aSerial 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. 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