The driving force for protein crystallization is the supersaturation. In th
e case of crystal growth in a hanging drop, the supersaturation at early ti
mes is controlled by the dynamics of solvent evaporation and is largely ind
ependent of the rate of appearance of the crystals. This permits the equati
ons of Johnson, Mehl, Avrami, and Kolomogrov to be integrated using the cla
ssic model for crystal nucleation and the spiral dislocation model for crys
tal growth. As results one obtains a formula for the number of crystals in
the drop and another formula for their average size. The parameters in thes
e formulae include either explicitly or implicitly the protein mass, temper
ature, pH, and ionic strength, which are the independent variables known ex
perimentally to influence the overall rate of protein crystallization. (C)
1999 Published by Elsevier Science B.V. All rights reserved.