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TitleCryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar.
Journal, issue, pagesSci Adv, Vol. 10, Issue 7, Page eadl4628, Year 2024
Publish dateFeb 16, 2024
AuthorsTim K Esser / Jan Böhning / Alpcan Önür / Dinesh K Chinthapalli / Lukas Eriksson / Marko Grabarics / Paul Fremdling / Albert Konijnenberg / Alexander Makarov / Aurelien Botman / Christine Peter / Justin L P Benesch / Carol V Robinson / Joseph Gault / Lindsay Baker / Tanmay A M Bharat / Stephan Rauschenbach /
PubMed AbstractNative mass spectrometry (MS) has become widely accepted in structural biology, providing information on stoichiometry, interactions, homogeneity, and shape of protein complexes. Yet, the fundamental ...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.
External linksSci Adv / PubMed:38354247 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 2.6 Å
Structure data

18244

8q7y

EMDB-18244, PDB-8q7y:
ESIBD structure of beta-galactosidase
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-18245: Plunge-frozen (control) map of beta-galactosidase
Method: EM (single particle) / Resolution: 2.3 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsHYDROLASE / Lactase / Beta-galactosidase / cryo-EM / native MS

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