United Kingdom, France, United States, European Union, 10 items
Organization
Grant number
Country
Biotechnology and Biological Sciences Research Council (BBSRC)
EP/V051474/1
United Kingdom
Medical Research Council (MRC, United Kingdom)
MC UP 1201/31
United Kingdom
Human Frontier Science Program (HFSP)
RGY0074/2021
France
Engineering and Physical Sciences Research Council
EP/V026623/1
United Kingdom
The Vallee Foundation Inc.
United States
European Molecular Biology Organization (EMBO)
European Union
Leverhulme Trust
United Kingdom
The Lister Institute of Preventive Medicine
United Kingdom
Wellcome Trust
104633/Z/14/Z
United Kingdom
Royal Society
NIF/R1/192285
United Kingdom
Citation
Journal: Sci Adv / Year: 2024 Title: Cryo-EM of soft-landed β-galactosidase: Gas-phase and native structures are remarkably similar. Authors: Tim K Esser / Jan Böhning / Alpcan Önür / Dinesh K Chinthapalli / Lukas Eriksson / Marko Grabarics / Paul Fremdling / Albert Konijnenberg / Alexander Makarov / Aurelien Botman / Christine ...Authors: Tim 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 / 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 ...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.
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