An orthorhombic crystal form of subtilisin BPN' variant s88 exhibits a systematic variation in growth rates of its three unique faces, resulting in pronounced variations in crystal morphology as a function of the ionic strength (Gallagher et al., J. Crystal Growth 193 (1998) 665). We have sought to explain these observations by performing energetics calculations using the full structural details of the protein. The approach of correlating growth rates with the strength of interactions of molecular pairs in the crystal proved unsatisfactory. The attachment of protein molecules to growing crystal faces is a stochastic process: a protein molecule samples numerous configurational (orientational and translational) states before attaching to the crystal in a configuration consistent with the crystal symmetry. This search-and-bind process determines the rate of crystal growth. We present a simplified approach that mimics this dynamical process: we perform docking of a protein molecule with another protein molecule or a cluster of molecules. An analysis of the bound configurations reveals the presence of orientations that are incommensurate with the crystal symmetry but in which a protein molecule can also bind strongly to the crystal face. Such improperly oriented molecules can be thought of as competitive inhibitors, and their presence is shown to affect the growth rate. Thus procedures aimed at decreasing the effect of such competitive inhibition, or conversely increasing the specificity of protein-protein interactions forming the crystal, are expected to offer better control of crystal growth rates.