Concomitantly, statistics from the Protein Data Bank (PDB) and the Electron Microscopy Data Bank (EMDB) show a clear increase in the number of protein structures that are recovered through electron-based techniques. Transmission electron microscopy as a tool for both material and life science has recently seen revolutionary developments, driven by new types of electron detectors, computational data analysis, automation, and sample preparation. Detailed examples are provided in extensive supplementary code. Here, we introduce our analysis pipeline for SerialED data, and its implementation using the CrystFEL and diffractem program packages. However, SerialED also necessitates new techniques of data processing, which combine existing pipelines for rotation electron diffraction and serial X-ray crystallography with some more particular solutions for challenges arising in SerialED specifically. Similarly to serial X-ray crystallography, this approach leads to almost complete absence of radiation damage effects even for the most sensitive samples, and allows for a high level of automation. Serial electron diffraction (SerialED) is an emerging technique, which applies the snapshot data-collection mode of serial X-ray crystallography to three-dimensional electron diffraction (3D Electron Diffraction), forgoing the conventional rotation method. 4Department of Chemistry, University of Toronto, Toronto, ON, Canada.3Department of Physics, University of Toronto, Toronto, ON, Canada.2Centre for Structural Systems Biology, Department of Chemistry, University of Hamburg, Hamburg, Germany.1Max Planck Institute for the Structure and Dynamics of Matter, Center for Free-Electron Laser Science, Hamburg, Germany.Robert Bücker 1,2* † Pascal Hogan-Lamarre 1,3,4 † R.
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