Native mass spectrometry (nMS) is an increasingly popular technique for studying intact protein quaternary structure. When coupled with ion mobility, which separates ions based on their size, charge, and shape, it provides additional structural information on the protein complex of interest. We present here data from a novel prototype TIMS (trapped ion mobility spectrometry)-quadrupole-SID (surface-induced dissociation)-time of flight, TIMS-Q-SID-TOF, instrument for nMS. The modifications include changing the TIMS cartridge from concave to convex electrode geometry with a dual TIMS tunnel design and operating TIMS at 425 kHz radio frequency (RF) to improve the trapping efficiency for high mass-to-charge (