Surface-induced dissociation of protein complex ions in a modified electrostatic linear ion trap

Abstract

The electrostatic linear ion trap (ELIT) is a device that can provide mass analysis via frequency measurement, followed by Fourier transformation from the frequency domain to the time domain, or via time measurement in a multi-reflection time-of-flight measurement. ELIT devices have been demonstrated to be capable of relatively high mass measurement resolution as well as high-resolution ion isolation capabilities. We have been exploring the possibility of developing the ELIT geometry as a stand-alone high-performance tandem mass spectrometer for native mass spectrometry (MS) studies. In this context, it is desirable to use an activation method capable of dissociating the high-mass complexes encountered in native MS. To this end, we describe the implementation of surface-induced dissociation (SID) in an ELIT and describe initial results for protein complexes generated under native conditions in which ion isolation, fragmentation, and product ion mass analysis all occur within the ELIT.