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2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
Open accessAbstract
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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Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
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De novo modeling in cryo-EM density maps with Pathwalking
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DeepCryoPicker: fully automated deep neural network for single protein particle picking in cryo-EM
Al-Azzawi, A., Ouadou, A., Max, H., Duan, Y., Tanner, J. J., & Cheng, J. (2020) · BMC Bioinformatics · doi:10.1186/s12859-020-03809-7 · Cited by 74
Metadata
- Authors
- Bartesaghi, A., Merk, A., Banerjee, S., Matthies, D., Wu, X., Milne, J. L. S., & Subramaniam, S.
- Venue
- Science
- Published
- 2015-06-05
- Volume
- 348
- Issue
- 6239
- Pages
- 1147-1151
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1810581179
- Cited by
- 438
- References
- 1
- FWCI
- 40.10
- Type
- journal article
- Language
- en
- Open access
- green
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- Bartesaghi, A., Merk, A., Banerjee, S., Matthies, D., Wu, X., Milne, J. L. S., & Subramaniam, S. (2015). 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. Science. https://doi.org/10.1126/science.aab1576
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