Temperature dependence of protein solubility — determination and application to crystallization in X-ray capillaries

Abstract A scintillation method was developed for determinations of the temperature dependence of the solubility, and of nucleation induction times of proteins, in 50–100 μl volumes of solution. Solubility data for lysozyme and horse serum albumin were obtained for various combinations of pH and precipitant concentrations. These data and the nucleation induction information were used for dynamic crystallization control, that is, for the controlled separation of nucleation and growth stages. Individual lysozyme and horse serum albumin crystals were grown in 15–20 μl solution volumes contained in X-ray capillaries.

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