We describe a set of simple devices for surface-induced dissociation of protein complexes on three instrument platforms. All of the devices use a novel yet simple split lens geometry that is minimally invasive (requiring a few mm along the ion path axis) and easier to operate than prior generations of devices. The split lens is designed to be small enough to replace the entrance lens of a Bruker FT-ICR collision cell, the dynamic range enhancement (DRE) lens of a Waters Q-IM-TOF, or the exit lens of a transfer multipole of a Thermo Scientific Extended Mass Range (EMR) Orbitrap. The split lens used for SID is an order of magnitude smaller than the first-generation SID devices developed in our laboratory and approximately 5x smaller than the second-generation devices developed on the Q-IM-TOF and FT-ICR. Despite the decrease in size and reduction in number of electrodes to 3 (from 10-12 in Gen 1 and ~6 in Gen 2), we show sensitivity improvement in a variety of cases across all platforms while also maintaining SID capabilities across a wide mass and energy range. The coupling of SID, high resolution, and ion mobility is demonstrated for a variety of protein complexes of varying topologies.
