We are studying liquid structure, phase separation and cluster formation in aqueous solutions of the bovine eye lens protein, gamma-B crystallin, as functions of charge and ionic strength. The role of charge in lens protein phase separation is important for understanding cataract, since changes in lens protein charge, known to occur during aging, are expected to affect solution stability. At 0.24M ionic strength, decreasing pH from 7.1 to 5.5 and thereby increasing net protein charge from +2 to +6 lowers the gamma-B upper consolute temperature by 8 degrees C. Further increasing gamma-B charge to +9 at pH 4.5 changes effective gamma-B interactions from attractive to repulsive at accessible temperatures, as observed by small-angle neutron scattering, and no phase separation is observed. Lowering ionic strength at pH 4.5 further increases repulsive interactions. Low-angle neutron scattering from gamma-B crystallin near phase separation is well-fit by the Baxter sticky-sphere model, but larger-angle scattering may reflect anisotropy of protein features and interactions. We compare small-angle scattering results for gamma-B crystallin at low ionic strength to evidence for lysozyme cluster formation under analogous solution conditions.