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Cryo-electron microscopy (cryo-EM) is rapidly emerging as a powerful tool for protein structure determination at high resolution. Here we report the structure of a complex between Escherichia coli ??-galactosidase and the cell-permeant inhibitor phenylethyl ??-D-thiogalactopyranoside (PETG), determined by cryo-EM at an average resolution of ~2.2 angstroms (??). Besides the PETG ligand, we identified densities in the map for ~800 water molecules and for magnesium and sodium ions. Although it is likely that continued advances in detector technology may further enhance resolution, our findings demonstrate that preparation of specimens of adequate quality and intrinsic protein flexibility, rather than imaging or image-processing technologies, now represent the major bottlenecks to routinely achieving resolutions close to 2 ?? using single-particle cryo-EM.

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OK, all this cryo-electron microscopy stuff is great, new protein structures, things that are huge, that can’t be crystallized, fine, fine: but when, the medicinal chemists in the audience ask, will we be able to use it for structure-based drug discovery?...