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Structural Biology: CryoEM’s Resolution Revolution
In what has come to be known as the resolution revolution, cryoelectron microscopy (cryoEM) is producing structures of proteins and biological complexes at resolutions that rival more-established techniques. With it, researchers are plumbing the biology of critical cellular machinery, discovering such details as where on a protein surface compounds bind, how receptor proteins are activated, and how disease-associated proteins interact with cellular structures.
Research institutions and drug companies across the world are racing to build capacity and hire scientists with relevant expertise. There is a renewed push for standardized, automated sample preparation and ‘vitrification’ techniques so that ever more macromolecular secrets can be revealed. But cryoEM improvements, fueled mainly by better electron detectors, have moved so fast that researchers’ mindsets, workflows, and computational tools are struggling to catch up. Some techniques, adapted from other structural methods, overlook the nuances of cryoEM-based data. Others are reaching the limits of proteins and complexes to which they can be applied.
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