Thaumatin, an intensely sweet protein, crystallizes rapidly in the presence of tartrate ions. The ease with which crystals form has led to the use of thaumatin over the past decade as a model system for the study of protein crystallization. The available data on the solubility of this protein, however, are inconsistent. We have purified thaumatin and determined its solubility with the l and d enantiomers of the tartrate ion. We find that the crystal habit and solubility are significantly different for the two precipitants: the solubility increases with temperature in l -tartrate, while it decreases with temperature in d -tartrate. Our results suggest that the chirality of precipitants is an important factor that should be controlled when determining the solubility of proteins.
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Asherie et al. (2008) studied this question.
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