Concluding Remarks

Purification of genome-loaded recombinant adeno-associated viral (full rAAV) capsids from empty capsids is challenging. The current purification technology has low yields (typically ~50%). This presentation discusses the potential of using crystallization for the separation of full and empty capsids, with the objective of achieving >90% yield. We propose an efficient method for purification of full rAAVs based on preferential crystallization. We have thoroughly mapped out the crystallization phase diagrams for full and empty rAAV capsid, which shows very large crystal nucleation and growth regions as a function of pH and precipitant concentrations. The phase diagrams and kinetic analyses for multiple serotypes indicate that preferential crystallization is feasible.