2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor

American Association for the Advancement of Science (AAAS) - Tập 348 Số 6239 - Trang 1147-1151 - 2015
Alberto Bartesaghi1, Alan Merk1, Soojay Banerjee1, Doreen Matthies1, Xiongwu Wu2, Jacqueline L.S. Milne1, Sriram Subramaniam1
1Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
2Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA

Tóm tắt

Pushing the limits of electron microscopy

Recent advances in cryo–electron microscopy (cryo-EM) allow structures of large macromolecules to be determined at near-atomic resolution. So far, though, resolutions approaching 2 Å, where features key to drug design are revealed, remain the province of x-ray crystallography. Bartesaghi et al. achieved a resolution of 2.2 Å for a 465-kD ligand-bound protein complex using cryo-EM. The density map is detailed enough to show close to 800 water molecules, magnesium and sodium ions, and precise side-chain conformations. These results bring routine use of cryo-EM in rational drug design a step closer.

Science , this issue p. 1147

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American Association for the Advancement of Science (AAAS)

Tập 348 Số 6239

1147-1151

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