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TitleThree-dimensional structure determination of protein complexes using matrix-landing mass spectrometry.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 2276, Year 2022
Publish dateApr 27, 2022
AuthorsMichael S Westphall / Kenneth W Lee / Austin Z Salome / Jean M Lodge / Timothy Grant / Joshua J Coon /
PubMed AbstractNative mass spectrometry (MS) is increasingly used to provide complementary data to electron microscopy (EM) for protein structure characterization. Beyond the ability to provide mass measurements of ...Native mass spectrometry (MS) is increasingly used to provide complementary data to electron microscopy (EM) for protein structure characterization. Beyond the ability to provide mass measurements of gas-phase biomolecular ions, MS instruments offer the ability to purify, select, and precisely control the spatial location of these ions. Here we present a modified Orbitrap MS system capable of depositing a native MS ion beam onto EM grids. We further describe the use of a chemical landing matrix that preserves the structural integrity of the deposited particles. With this system we obtain a three-dimensional reconstruction of the 800 kDa protein complex GroEL from gas-phase deposited GroEL ions. These data provide direct evidence that non-covalent protein complexes can indeed retain their condensed-phase structures following ionization and vaporization. Finally, we describe how further developments of this technology could pave the way to an integrated MS-EM technology with promise to provide improved cryo-EM sample preparation over conventional plunge-freezing techniques.
External linksNat Commun / PubMed:35478194 / PubMed Central
MethodsEM (single particle)
Resolution15.0 Å
Structure data

EMDB-26222: 3D Structure Determination of GroEL Protein Complexes using Matrix-Landing Mass Spectrometry
Method: EM (single particle) / Resolution: 15.0 Å

Source
  • Escherichia (bacteria)

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