Modulating the crystal size and morphology of in meso-crystallized lysozyme by precisely controlling the water channel size of the hosting mesophase

We explore the effects of increased protein mobility inside the aqueous channels of ordered lyotropic liquid crystals (LLC) of cubic Pn3m symmetry on the process of in meso crystallization of lysozyme proteins. The protein confinement within the channels is released by swelling the aqueous domains by doping the mesophase with a hydration-modulating agent that causes a near twofold increase in the diameter of the water channels. By means of small angle X-ray scattering and cross-polarized optical microscopy, we then show that increased diffusion of both protein and water molecules within the bulk hosting LLC leads to the formation of not only larger protein crystals but also crystals belonging to different polymorphic forms.