The well-established and preeminent method used to fragment ions in a mass spectrometry (MS) experiment is collision-induced dissociation (CID).¹  This is a standard operating procedure in most commercial mass spectrometers with undoubted benefits in reproducibility especially in ‘omic applications.^2–4  In a classic CID experiment, a given molecular ion is accelerated through a region of the mass spectrometer filled with an inert gas. Fragmentation proceeds via collisions which results in the transfer of kinetic energy to break the weakest bonds in a given analyte. This preference for weaker bonds can be disadvantageous, for example in cleaving post-translational modifications (PTMs), and when applied to noncovalent protein complexes, the energy deposited prior to fragmentation substantially perturbs the tertiary structure. CID is common in bottom-up proteomics investigations where peptide ions cannot inform on the tertiary or quaternary structure of the protein but do provide valuable information to map the primary structure.