6CVM

Atomic resolution cryo-EM structure of beta-galactosidase

6CVM の概要

• エントリーDOI: 10.2210/pdb6cvm/pdb
• EMDBエントリー: 7770
• 分子名称: Beta-galactosidase, 2-phenylethyl 1-thio-beta-D-galactopyranoside, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: drift correction, radiation damage, drug discovery, precision medicine, computer-aided drug discovery, hydrolase
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 466303.97

構造登録者

Subramaniam, S.,Bartesaghi, A.,Banerjee, S.,Zhu, X.,Milne, J.L.S. (登録日: 2018-03-28, 公開日: 2018-05-30, 最終更新日: 2024-03-13)

主引用文献

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

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: 29754826
DOI: 10.1016/j.str.2018.04.004

実験手法

ELECTRON MICROSCOPY (1.9 Å)