Abstract
We present a de novo model building approach that combines predicted backbone conformations with side-chain density-fit to accurately assign sequence into density maps. We show this method yields accurate models for six experimental maps at 3.3–4.8 Å resolution, and produces a nearly complete model for an unsolved map containing a 660-residue hetero-dimeric protein. This method should enable rapid and reliable protein structure determination from near-atomic resolution cryo-EM maps.
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