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Updated: Jun 24, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
Published on: April 17, 2017
Digital ion trap mass spectrometer for probing the structure of biological macromolecules by gas phase X-ray
Bryan J McCullough1, Andrew Entwistle, Ikuo Konishi
1Michael Barber Centre for Mass Spectrometry, Manchester Interdisciplinary Biocentre, The University of Manchester, Manchester, UK.
Abstract:
Small-angle X-ray scattering is a technique for the characterization and structural analysis of a variety of materials including biological macromolecules and polymers. For the conformational analysis of proteins, the interaction between sample and X-rays is generally performed when the proteins are present in solution. Here a three-dimensional digital ion trap interfaced with a high intensity X-ray source is built to prove that X-ray scattering can be performed on ions isolated in gas-phase. Initial experiments on an unresolved ion population of multiply charged cytochrome C ions indicate that a small-angle X-ray scattering signal can be detected and that partial structural information can be extracted about the overall molecular structure of protein ions.
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