6CVM
Atomic resolution cryo-EM structure of beta-galactosidase
Summary for 6CVM
| Entry DOI | 10.2210/pdb6cvm/pdb |
| EMDB information | 7770 |
| Descriptor | Beta-galactosidase, 2-phenylethyl 1-thio-beta-D-galactopyranoside, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | drift correction, radiation damage, drug discovery, precision medicine, computer-aided drug discovery, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 4 |
| Total formula weight | 466303.97 |
| Authors | Subramaniam, S.,Bartesaghi, A.,Banerjee, S.,Zhu, X.,Milne, J.L.S. (deposition date: 2018-03-28, release date: 2018-05-30, Last modification date: 2024-03-13) |
| Primary citation | Bartesaghi, A.,Aguerrebere, C.,Falconieri, V.,Banerjee, S.,Earl, L.A.,Zhu, X.,Grigorieff, N.,Milne, J.L.S.,Sapiro, G.,Wu, X.,Subramaniam, S. Atomic Resolution Cryo-EM Structure of beta-Galactosidase. Structure, 26:848-, 2018 Cited by PubMed Abstract: The advent of direct electron detectors has enabled the routine use of single-particle cryo-electron microscopy (EM) approaches to determine structures of a variety of protein complexes at near-atomic resolution. Here, we report the development of methods to account for local variations in defocus and beam-induced drift, and the implementation of a data-driven dose compensation scheme that significantly improves the extraction of high-resolution information recorded during exposure of the specimen to the electron beam. These advances enable determination of a cryo-EM density map for β-galactosidase bound to the inhibitor phenylethyl β-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at ∼ 1.5 Å resolution. Using this density map in conjunction with constrained molecular dynamics simulations provides a measure of the local flexibility of the non-covalently bound inhibitor and offers further opportunities for structure-guided inhibitor design. PubMed: 29754826DOI: 10.1016/j.str.2018.04.004 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.9 Å) |
Structure validation
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