Mainz 2026 – wissenschaftliches Programm

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MS: Fachverband Massenspektrometrie

MS 3: Actinide Analysis

MS 3.1: Hauptvortrag

Dienstag, 3. März 2026, 11:00–11:30, N 6

Flying viruses - Native mass spectrometry meets X-rays — •Charlotte Uetrecht — CSSB Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron DESY & Leibniz Institute of Virology (LIV) & University of Lübeck, Notkestraße 85, 22607 Hamburg, Germany — Institute of Chemistry and Metabolomics, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany

Native mass spectrometry (MS) enables ionisation and transfer of structurally intact non-covalent protein complexes into the gas-phase. As such, it is a perfect tool to study proteins and their assembly intermediates in a mass and conformation specific manner, albeit with limited structural resolution. Accordingly, other experimental approaches such as X-ray diffractive imaging are necessary to get a full understanding of proteins, their assemblies and dynamic processes. Therefore, it seems natural to combine native MS with X-ray diffraction in the gas phase. In particular, well established methods from MS like m/z selection, ion trapping or ion mobility are incorporated in the MS SPIDOC sample delivery system. In contrast to conventional diffractive imaging of crystallised proteins, the proteins here are delivered as single particles without the need for crystallisation. This increases naturally the requirement on the X-ray source: high-resolution single-particle X-ray diffractive imaging (SPI) can only be conducted at X-ray free electron lasers, lower resolution information can be obtained from small angle X-ray scattering (SAXS) at synchrotrons. This talk highlights first results from leveraging such synergies, and how this will improve our understanding of virus structure and dynamics.

Keywords: X-ray diffraction; X-ray spectroscopy; biomolecular mass spectrometry; biophysics; structural biology