Uncovering the solution structure of habit related polymorphic amino acid - DL-methionine

Understanding crystal structure during the crystallisation process is of paramount importance for uncovering self-assembly mechanisms and kinetics. The link between polymorph, habit and crystallisation conditions is still not fully understood but is necessary for the optimisation of physicochemical properties such as dissolution rate of pharmaceuticals. We have uncovered a non-linear relationship between anti-solvent ratio and polymorphic / habit expression in the cooling crystallisation of the essential amino acid DL-methionine, in contrast to a previous study on this material. Using neutron diffraction we will interrogate the liquid structure before crystallisation occurs to see how the differences in anti-solvent fraction are influencing the final polymorphic and habit (shape) form. This will then be compared to in situ diffraction studies at Diamond Light Source investigating detailed single crystal XRD with simultaneous 3D habit analysis in a custom flow crystallisation apparatus.