Gamma D-crystallin is one of the major proteins in the lens. In the present study, it has been expressed using E. coli and purified with ion exchange chromatography. Initial crystallization of this protein has been carried out in Eppendorf tubes to determine suitable concentrations for observable crystals. Further crystallization is carried out on an automated stage and with varying solution conditions.
Crystallization of a gamma D-crystallin could be predicted by measuring pre-crystallization or nucleation determinants using light scattering techniques. In this work an effort is made to correlate the crystallization habits of gamma D-crystallin and parameters observed with light scattering.