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| Title | 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. |
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| Journal, issue, pages | Science, Vol. 348, Issue 6239, Page 1147-1151, Year 2015 |
| Publish date | Jun 5, 2015 |
 Authors | Alberto Bartesaghi / Alan Merk / Soojay Banerjee / Doreen Matthies / Xiongwu Wu / Jacqueline L S Milne / Sriram Subramaniam /  |
| PubMed Abstract | 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- ...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. |
 External links | Science / PubMed:25953817 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.2 Å |
| Structure data | |
| Chemicals |  ChemComp-PTQ:  ChemComp-MG:  ChemComp-NA:  ChemComp-HOH: |
| Source |
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 Keywords | HYDROLASE / NEAR-ATOMIC / NEAR-ATOMIC RESOLUTION CRYO-ELECTRON MICROSCOPY / SINGLE- PARTICLE CRYO-EM / PROTEIN COMPLEXES / PETG |
escherichia coli k-12 (bacteria)