The protein is crystallized in the presence of a mineral surface exhibiting a close match of its crystalline lattice to that of the desired protein, and a mismatch to the crystals of the protein impurities. Experiments suggest that the mineral surface causes a reduction in the level of supersaturation needed to crystallize the protein. Crystallization in the presence of exogenous minerals exhibiting a close lattice match may enable the production of protein crystals of higher quality and purity. Such crystals are valuable in studies on tertiary structure by diffraction techniques and on the rational design of new drugs. Crystallization in the presence of mineral surfaces may also result in significantly higher protein purity compared to that achieved by traditional crystallization methods.
Protein crystallization is currently more art than science.
The outcome of protein crystallization procedures relies heavily on chance. This method reduces variability and may lead to protein crystals of higher quality, which are needed in various applications. The described method also appears to produce purer crystals than conventional crystallization procedures. A novel and unusual feature is the utilization of a unique driving force for inducing protein crystallization and enhancing purification. The apparent efficacy of the process has been demonstrated at the laboratory level.