Three-dimensional structure determination of protein complexes using matrix-landing mass spectrometry

Michael S. Westphall, Kenneth W. Lee, Austin Z. Salome, Jean M. Lodge, Timothy Grant () and Joshua J. Coon ()
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Michael S. Westphall: University of Wisconsin-Madison
Kenneth W. Lee: University of Wisconsin-Madison
Austin Z. Salome: University of Wisconsin-Madison
Jean M. Lodge: University of Wisconsin-Madison
Timothy Grant: University of Wisconsin-Madison
Joshua J. Coon: University of Wisconsin-Madison

Nature Communications, 2022, vol. 13, issue 1, 1-6

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-29964-4

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