Table 3.

Equilibrium dissociation constants of PrgX, PrgX‐I, and PrgX‐C binding to LT‐DNA

Protein‐DNA	K D (nmol L−1)
PrgX‐C‐LT DNA	K = 0.43 ± 0.10
PrgX‐I‐LT DNA	K = 0.21 ± 0.052
PrgX‐LT DNA	K xbs1 = 4.04 ± 3.36
	K xbs2 = 341.85 ± 377.5

Equilibrium dissociation constants were estimated from binding polynomials presented in the Supporting Information. Values are the mean ± SD of three independent EMSA experiments similar to those depicted in Figure 7. PrgX binding to LT produced two shifts, with K _xbs1 being the K _D of binding to XBS1 site, and K _xbs2 is the K _D of binding to XBS2 site. Binding of PrgX‐C or PrgX‐I tetramers to LT produced a single shifted species, which corresponds to the second shift observed with Apo‐PrgX.