2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor.
Journal Article (Journal Article)
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 β-galactosidase and the cell-permeant inhibitor phenylethyl β-D-thiogalactopyranoside (PETG), determined by cryo-EM at an average resolution of ~2.2 angstroms (Å). 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 Å using single-particle cryo-EM.
Full Text
Duke Authors
Cited Authors
- Bartesaghi, A; Merk, A; Banerjee, S; Matthies, D; Wu, X; Milne, JLS; Subramaniam, S
Published Date
- June 2015
Published In
Volume / Issue
- 348 / 6239
Start / End Page
- 1147 - 1151
PubMed ID
- 25953817
Pubmed Central ID
- PMC6512338
Electronic International Standard Serial Number (EISSN)
- 1095-9203
International Standard Serial Number (ISSN)
- 0036-8075
Digital Object Identifier (DOI)
- 10.1126/science.aab1576
Language
- eng