We have performed multiangle static and dynamic light scattering studies of lysozyme solutions at pH=4.7. The Rayleigh ratio R(theta) and the collective diffusion coefficient D-c were determined as function of both protein concentration c(p) and salt concentration c(s) with two different salts. At low salt concentrations, the scattering ratio Kc(p)/R(theta) and diffusivity increased with protein concentration above the values for a monomeric, ideal solution. With increasing salt concentration this trend was eventually reversed. The hydrodynamic interactions of lysozyme in solution, extracted from the combination of static and dynamic scattering data, decreased significantly with increasing salt concentration. These observations reflect changes in protein interactions, in response to increased salt screening, from net repulsion to net attraction. Both salts had the same qualitative effect, but the quantitative behavior did not scale with the ionic strength of the solution. This indicates the presence of salt specific effects. At low protein concentrations, the slopes of Kc(p)/R(theta) and D-c vs c(p) were obtained. The dependence of the dopes on tonic strength was modeled using a DLVO potential for colloidal interactions of two spheres, with the net protein charge Ze and Hamaker constant A(H) as fitting parameters. The model reproduces the observed variations with ionic strength quite well. Independent fits to the static and dynamic data, however, led to different values of the fitting parameters. These and other shortcomings suggest that colloidal interaction models alone are insufficient to explain protein interactions in solutions.