CLASSICAL NUCLEATION THEORY APPLIED TO THE HETEROGENOUS NUCLEATION OF PROTEIN CRYSTALS

摘要

Crystallisation is commonly employed in the separation and purification of proteins.rnHowever, some proteins are very difficult to crystallise. The high degree ofrnsupersaturation typically required for protein crystallisation results in relatively fastrncrystal growth during which impurities are likely to be incorporated in the crystal.rnPrevious research has shown that mineral substrates have reduced the time forrnnucleation, which indicates a reduction in the supersaturation required forrnnucleation. In addition, an increase in the purity of lysozyme crystals grown byrnvapor diffusion has been correlated with close lattice matching to mineral substrates.rnIn this paper, classical nucleation theory is applied to help interpret results ofrnexperiments involving lysozyme and carefully selected mineral substrates.rnPreliminary results are presented studying the effect of the mineral’s surfacernchemistry as well as lattice matching on the induction time for nucleationrninvestigated using video microscopy.