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Cited by 438

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

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

Open access
Bartesaghi, Alberto, Merk, Alan, Banerjee, Soojay, Matthies, Doreen, Wu, Xiongwu, Milne, Jacqueline L. S., Subramaniam, Sriram·2015·Science

Abstract

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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Crossref · 10.1126/science.aab1576

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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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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