Stability constants K and half saturation constants Ks for binding of proteins with and without His6-tags to membrane channels formed by anthrax PA63 and C2II.

Stability constants K and half saturation constants Ks for the binding of His6-tagged and untagged EF, LF, C2I, gpJ or EDIN to PA63- or C2II-channels in lipid bilayer membranes. The membranes were painted from 1% (w/v) diphytanoyl phosphatidylcholine dissolved in n-decane. The aqueous phase contained 150 mM KCl, buffered to pH between 5.5 and 6 using 10 mM MES-KOH; T = 20°C. Measurements were performed at a membrane potential of 20 mV. The data represent the means (± SD) of at least three individual titration experiments. KS is the half saturation constant, i.e. KS = 1/K. Stability constants given in bold were adjusted to the voltage dependent behavior of binding. (* taken from [21] ** taken from [43]).