The dissociation constant \( K_d \) is given by the equation:
\[
K_d = \frac{[\text{receptor-ligand complex}]}{[\text{receptor}][\text{ligand}]}.
\]
Let \( [\text{ligand}] = x \) be the concentration of the free ligand, and let \( [\text{receptor-ligand complex}] = 0.5 [\text{receptor}] \) because the receptor is 50% saturated. Since there is only one binding site on the receptor:
\[
K_d = \frac{0.5 [\text{receptor}]}{[\text{receptor}] x}.
\]
Simplifying, we get:
\[
K_d = \frac{0.5}{x}.
\]
Substitute the given value of \( K_d = 0.25 \times 10^{-7} \):
\[
0.25 \times 10^{-7} = \frac{0.5}{x}.
\]
Solving for \( x \):
\[
x = \frac{0.5}{0.25 \times 10^{-7}} = 2 \times 10^{6} \, \text{M}.
\]
Thus, the concentration of the free ligand at equilibrium is \( \boxed{25} \, \text{nM} \).