Crystallization of Thaumatin
Since thaumatin crystallizes rapidly and easily in the presence of tartrate ions, thaumatin-tartrate mixtures are frequently used as model systems to study protein crystallization. Interestingly, the solubility of thaumatin, its crystal habit, and mechanism of crystal formation is dependent upon the chirality of precipitant used. When crystalized with L- tartrate, thaumatin forms bipyramidal crystals and displays a solubility that increases with temperature; with D- and meso-tartrate, it forms stubby and prismatic crystals and displays a solubility that decreases with temperature. This suggests control of precipitant chirality may be an important factor in protein crystallization in general.
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