Figure tracks CRP's SID monomer product average charge state as a function of cone voltage. Evident from the plot is the statistically significant (*, p < 0.05) increase in monomer average charge state with increased isCA, which agrees with similar work from the Wysocki lab in 2015, performed on a Waters Synapt G2. The interpretation given at that time is that the cone isCA process, at 160 V, both rearranges the protein such that the measured CCS is smaller (shorter drift time in our data), while also causing a monomeric subunit to partially elongate but remain non-covalently bound to the remaining subunits. The SID process then allows that elongated monomer to abstract additional charge as it leaves the protein complex. This is also consistent with what we observed for SA. Returning to the interesting regions between 80 -110 V, the average monomer charge state increases at a faster rate than it did between 10 -80 V. Based on the discussion above, this could be due to the increase in secondary fragmentation from energy deposition during isCA followed by SID. As the CIx plot reflects quaternary structure collapse, the average monomer charge state appears to approach a rollover point to a constant value. Unfortunately, this rollover point is not completed due to the upper limit on the cone voltage.