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Simple and Minimally Invasive SID Devices for Native Mass Spectrometry

preprint
revised on 26.04.2020 and posted on 27.04.2020 by Dalton Snyder, Erin Panczyk, Arpad Somogyi, Desmond Kaplan, Vicki Wysocki

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.

Funding

S10 OD018507

Resource for Native Mass Spectrometry Guided Structural Biology

National Institute of General Medical Sciences

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History

Email Address of Submitting Author

snyder.1720@osu.edu

Institution

The Ohio State University

Country

United States

ORCID For Submitting Author

0000-0003-2154-5002

Declaration of Conflict of Interest

None

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in Analytical Chemistry

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