Journal
ANALYTICAL CHEMISTRY
Volume 92, Issue 16, Pages 11195-11203Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.0c01657
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Funding
- NIH [R01 GM120425, R01 GM120923, S10 OD018507]
- NIH P41 Resource for Native Mass Spectrometry Guided Structural Biology [P41GM128577]
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We describe a set of simple devices for surface-induced dissociation of proteins and 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 millimeters along the ion path axis) and is 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. Despite the decrease in size and reduction in number of electrodes to 3 (from 10 to 12 in Gen 1 and similar to 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.
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