Supplementary Figure 1: Multiangle light-scattering experiments.
From: Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor
In line size exclusion chromatography and multi angle light scattering (SEC-MALS) experiments were performed on various FliG constructs. 0.5 ml of purified protein at a concentration of 5 mg /ml was injected onto a 23 ml Superdex S200 size exclusion chromatography column with a flow rate of 0.5 ml/min. For all constructs, the majority of protein eluted in a single dominant elution peak. The absorbance at 280 nm and the molecular weight deduced from light scattering data from these peaks are shown for full-length FliG (blue), FliGMC (red) and FliGNM (green). Average experimentally determined molecular weight and polydispersity are recorded in the boxes. The correspondence between experimental and theoretical molecular weights, and low measured polydispersity, demonstrate that FliG proteins in the major elution peak are monodisperse and monomeric.
