Native ion mobility-mass spectrometry (IM-MS) is widely recognized as an important characterization technique for structural biology, but the performance metrics, <i>viz</i>. mobility and mass resolution, of commercially-available IM-MS instruments fall short of that needed for studies of intact macromolecule complexes. To circumvent these limitations, we have designed and developed a novel Fourier transform-IM-Orbitrap instrument that is capable of increased resolving power in both mobility and mass domains. The instrument design overcomes inherent duty-cycle mismatch for drift tube mobility coupled to Orbitrap analyzers while retaining capabilities for first principles determination of rotationally-averaged collision cross-sections. The instrument design also incorporates capabilities for CID and SID studies of both mobility- and mass-selected ions. This presentation will describe the novel features of the instrument and results from recent studies that illustrate the benefits of high mass resolution and accurate determinations of collision cross sections of large proteins and intact protein complexes.<br/>

Fourier transform ion mobility-Orbitrap spectrometer for native mass spectrometry

2019 Fall National Meeting

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