  Asymmetric patchy particle models have recently been shown to describe the
crystallization of small globular proteins with near quantitative accuracy.
Here, we investigate how asymmetry in patch geometry and bond energy generally
impact the phase diagram and nucleation dynamics of this family of soft matter
models. We find the role of the geometry asymmetry to be weak, but the energy
asymmetry to markedly interfere with the crystallization thermodynamics and
kinetics. These results provide a rationale for the success and occasional
failure of George and Wilson's proposal for protein crystallization conditions
as well as physical guidance for developing more effective protein
crystallization strategies.
