Native mass spectrometry (nMS), particularly in combination with unique activation methods and ion mobility spectrometry (IM), has proven a powerful structural biology technique for investigating topology, stoichiometry, and conformations of proteins and their complexes. Trapped ion mobility spectrometry (TIMS) is a high-resolution ion mobility spectrometry technique that was first introduced by Park and co-workers in 2011. Unlike traditional drift tube ion mobility cells (DTIMS) which use ions flying through a stationary gas in the drift tube, TIMS separates ions by using an opposing electric field and a moving column of gas to measure the analyte's ion mobility. TIMS has been coupled to Q-TOF and FT-ICR mass spectrometers and is widely applied in proteomics and metabolomics, including cross-linking mass spectrometry. Recently, Panczyk et al. demonstrated that a commercial TIMS-Q-TOF can perform nMS analysis on protein complexes up to 60 kDa with TIMS. Borotto and co-workers showed that a commercial TIMS-Q-TOF could also characterize protein structure up to 66 kDa by top-down sequencing and collision-induced unfolding by activation within the TIMS cartridge. Bleiholder and co-workers used a modified tandem TIMS-Q-TOF to characterize the structure of a glycoprotein, avidin, and small proteins. Fernandez-Lima and co-workers reported that a modified convex TIMS cartridge with a low radio frequency (RF) driver improves the ion mobility analysis of TIMS up to 800 kDa with a single peak resolution (Rp) of 85 compared to DTIMS with an Rp of 60 for protein complexes around or above 200 kDa. Because nMS users and applications are continuing to expand , and coupling it with IMS provides additional protein and protein complex structural information , we aimed to adapt a TIMS platform to perform nMS for studying and understanding large, complex protein structures up to the mega-Dalton (MDa) range with a high energy deposition tandem mass spectrometry (MS/MS) activation method, surface-induced dissociation (SID). The Wysocki lab has extended SID development to investigate protein structure and subcomplex connectivity for macromolecules. SID cleaves protein complexes at their weakest non-covalent interfaces and generates subunits with a charge state approximately proportional to the relative fragment ion mass. Currently, nMS has been applied to measure the structures of macromolecules in the MDa mass range, such as adeno-associated virus capsids (3.5 -5 MDa), antibody-bound capsids species (5 -17 MDa), and oligomerized 20S proteasome (0.7 -9.6 MDa), which are important for producing biotherapeutics. The Wysocki lab has demonstrated that SID is currently the only activation method capable of extensively dissociating these MDa biomolecules, making it a valuable tool for investigating the structure of AAVs. Here, we modified a commercial TIMS-Q-TOF mass spectrometer to study the structures of high molecular weight (MW) protein complexes. The modifications include changing the TIMS cartridge geometry to convex, lowering the RF frequency for both the TIMS cartridge and quadrupole, and installing a 2-lens SID device at the collision cell entrance. With these novel modifications, the application of nMS with ion mobility and SID on this prototype platform ranges from 50 kDa up to at least 4 MDa. This work presents the first demonstration coupling a high-mass TIMS cartridge, high-mass quadrupole, and unique activation technique (SID) to probe biomolecular structure on a mass spectrometry platform commercially designed for non-structural bottom-up proteomics experiments.