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It is shown that diffusion-limited classical nucleation theory (CNT) can berecovered as a simple limit of the recently proposed dynamical theory ofnucleation based on fluctuating hydrodynamics (Lutsko, JCP 136, 034509 (2012)).The same framework is also used to construct a more realistic theory in whichclusters have finite interfacial width. When applied to the dilutesolution/dense solution transition in globular proteins, it is found that theextension gives corrections to the the nucleation rate even for the case ofsmall supersaturations due to changes in the monomer distribution function andto the excess free energy. It is also found that the monomerattachement/detachment picture breaks down at high supersaturationscorresponding to clusters smaller than about 100 molecules. The results alsoconfirm the usual assumption that most important corrections to CNT can beacheived by means of improved estimates of the free energy barrier. The theoryalso illustrates two topics that have received considerable attention in therecent literature on nucleation: the importance sub-dominant corrections to thecapillary model for the free energy and of the correct choice of the reactioncoordinate.

Classical nucleation theory from a dynamical approach to nucleation