Structural highlights
Publication Abstract from PubMedThe 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 beta-galactosidase bound to the inhibitor phenylethyl beta-D-thiogalactopyranoside where the ordered regions are resolved at a level of detail seen in X-ray maps at approximately 1.5 A 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. Atomic Resolution Cryo-EM Structure of beta-Galactosidase.,Bartesaghi A, Aguerrebere C, Falconieri V, Banerjee S, Earl LA, Zhu X, Grigorieff N, Milne JLS, Sapiro G, Wu X, Subramaniam S Structure. 2018 May 10. pii: S0969-2126(18)30129-1. doi:, 10.1016/j.str.2018.04.004. PMID:29754826[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 06:31, 20 June 2018.