8Q7Y

ESIBD structure of beta-galactosidase

8Q7Y の概要

• エントリーDOI: 10.2210/pdb8q7y/pdb
• EMDBエントリー: 18244
• 分子名称: Beta-galactosidase (1 entity in total)
• 機能のキーワード: lactase, beta-galactosidase, cryo-em, native ms, hydrolase
• 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: 466290.00

構造登録者

Esser, T.,Boehning, J.,Bharat, T.A.M.,Rauschenbach, S. (登録日: 2023-08-17, 公開日: 2024-01-10, 最終更新日: 2024-03-06)

主引用文献

Esser, T.K.,Bohning, J.,Onur, A.,Chinthapalli, D.K.,Eriksson, L.,Grabarics, M.,Fremdling, P.,Konijnenberg, A.,Makarov, A.,Botman, A.,Peter, C.,Benesch, J.L.P.,Robinson, C.V.,Gault, J.,Baker, L.,Bharat, T.A.M.,Rauschenbach, S.
Cryo-EM of soft-landed beta-galactosidase: Gas-phase and native structures are remarkably similar.
Sci Adv, 10:eadl4628-eadl4628, 2024

PubMed Abstract: Native mass spectrometry (MS) has become widely accepted in structural biology, providing information on stoichiometry, interactions, homogeneity, and shape of protein complexes. Yet, the fundamental assumption that proteins inside the mass spectrometer retain a structure faithful to native proteins in solution remains a matter of intense debate. Here, we reveal the gas-phase structure of β-galactosidase using single-particle cryo-electron microscopy (cryo-EM) down to 2.6-Å resolution, enabled by soft landing of mass-selected protein complexes onto cold transmission electron microscopy (TEM) grids followed by in situ ice coating. We find that large parts of the secondary and tertiary structure are retained from the solution. Dehydration-driven subunit reorientation leads to consistent compaction in the gas phase. By providing a direct link between high-resolution imaging and the capability to handle and select protein complexes that behave problematically in conventional sample preparation, the approach has the potential to expand the scope of both native mass spectrometry and cryo-EM.

PubMed: 38354247
DOI: 10.1126/sciadv.adl4628

実験手法

ELECTRON MICROSCOPY (2.6 Å)