期刊
CRYSTAL GROWTH & DESIGN
卷 8, 期 6, 页码 1815-1817出版社
AMER CHEMICAL SOC
DOI: 10.1021/cg800276r
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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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