A. ExH at 0.027 μM (equivalent to 1.6 μM Dec binding locations, considering only the 60 high affinity sites at quasi-three fold symmetry axes) were mixed with Texas Red labeled, N-his-tagged, S90C Dec (TxR N-his Dec) at increasing μM concentrations, as indicated in the second line of the caption to the gel, at increasing concentrations, as indicated, or with unlabeled, N-his-tagged Dec. Samples were run on a native agarose gel and visualized by Coomassie Blue staining (top) or by fluorescence (excited with a transilluminator at 280 nm) (bottom). B. A representative fluorescence anisotropy assay of the binding of Texas Red labeled, N-his S90C Dec (at a concentration of 0.3 μM), was monitored during a titration with ExH. The abcissa axis gives the μM concentration of ExH multiplied by 60.