These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
2 files

Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer

submitted on 04.12.2018, 12:23 and posted on 05.12.2018, 15:32 by Zachary VanAernum, Joshua D. Gilbert, Mikhail E. Belov, Alexander A. Makarov, Stevan R. Horning, Vicki H. Wysocki
Herein we demonstrate the first adaptation of surface-induced dissociation in a modified high-mass range, high-resolution Orbitrap mass spectrometer. The SID device was designed to be installed in the Q-Exactive series of Orbitrap mass spectrometers with minimal disruption of standard functions. The performance of the SID-Orbitrap instrument has been demonstrated with several protein complex and ligand-bound protein complex systems ranging from 53 to 336 kDa. We also address the effect of ion source temperature on native protein-ligand complex ions as assessed by SID. Results are consistent with previous findings on quadrupole time-of-flight instruments and suggest that SID coupled to high-resolution MS is well-suited to provide information on the interface interactions within protein complexes and ligand-bound protein complexes.


IDBR: Type A. High-Performance Surface-induced Dissociation MS/MS

Directorate for Biological Sciences

Find out more...

Resource for Native Mass Spectrometry Guided Structural Biology

National Institute of General Medical Sciences

Find out more...


Email Address of Submitting Author


The Ohio State University


United States of America

ORCID For Submitting Author


Declaration of Conflict of Interest

M.E.B., A.A.M, and S.R.H. are employees of Thermo Fisher Scientific. The authors declare no additional conflicts of interest.