Energetic parameters of the interaction of SlmA with SBSs.

a∆G values correspond to the dissociation of the complex with two SlmA dimers bound to the SBS. In 50 mM Tris, 300 mM KCl, 2 mM MgCl2, pH 7.5.bKd,app, in dimer units, is an apparent Kd calculated from the value of ∆G divided by 2 and represents the concentration at which 50% of binding occurs.cIn working buffer with 100 mM KCl, ∆G for the interaction of SlmA with SBS17 was 21.6 (-0.6,+1.1) kcal/mol, assuming a complex with two dimers.Uncertainties were calculated by rigorous confidence limit testing at the 67% confidence level, using BIOEQS software.Energetic parameters of the interaction of SlmA with SBSs.