5A1A

2.2 A resolution cryo-EM structure of beta-galactosidase in complex with a cell-permeant inhibitor

5A1A の概要

• エントリーDOI: 10.2210/pdb5a1a/pdb
• EMDBエントリー: 2984
• 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: hydrolase, near-atomic, near-atomic resolution cryo-electron microscopy, single- particle cryo-em, protein complexes, petg
• 由来する生物種: ESCHERICHIA COLI K-12
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 467060.60

構造登録者

Bartesaghi, A.,Merk, A.,Banerjee, S.,Matthies, D.,Wu, X.,Milne, J.,Subramaniam, S. (登録日: 2015-04-29, 公開日: 2015-05-06, 最終更新日: 2024-05-08)

主引用文献

Bartesaghi, A.,Merk, A.,Banerjee, S.,Matthies, D.,Wu, X.,Milne, J.,Subramaniam, S.
2.2 A Resolution Cryo-Em Structure of Beta-Galactosidase in Complex with a Cell-Permeant Inhibitor
Science, 348:1147-, 2015

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-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.

PubMed: 25953817
DOI: 10.1126/SCIENCE.AAB1576

実験手法

ELECTRON MICROSCOPY (2.2 Å)