Abstract

An increasing number of density maps of macromolecular structures, including proteins and protein and DNA/RNA complexes, have been determined by cryo-electron microscopy (cryo-EM). Although lately maps at a near-atomic resolution are routinely reported, there are still substantial fractions of maps determined at intermediate or low resolutions, where extracting structure information is difficult. Of the structures deposited to the Electron Microscopy Data Bank (EMDB) between 2016 and 2019, over 50% were solved at intermediate resolution ranging between 5-10 Å, where detailed structures are not visible.

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