When polymers are added to a solution containing proteins, the protein may deposit as an amorphous precipitate or as crystals. Experimental evidence indicates that from a thermodynamic viewpoint, an amorphous precipitate should be treated as a liquid phase dense in the protein and crystals as true solids. To understand the conditions under which protein precipitation or crystallization may occur, Gibbs-ensemble Monte Carlo simulation and Gibbs-Duhem integration techniques are used to calculate the liquid-liquid and liquid-solid phase boundaries for protein precipitation induced by polymers. In these simulations, the system is modeled using the pseudo-one-component approximation with an appropriate potential of mean force. The critical point for fluid-fluid phase equilibrium disappears as the attractive part of the mean-force potential becomes very short ranged. The accuracy of the second-order Barker and Henderson perturbation theory is examined by company the phase diagram predicted using this method with the simulation results. Perturbation theory is able to predict the general trends observed in the simulations but not with quantitative accuracy. Perturbation theory is then used to examine a broader range of conditions for protein deposition.