Elemental Analysis and Crystallization of Protein Crystals

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Crystallization processes of a model substance : hen-egg white lysozyme were analyzed with laser scattering tomography, etching technique, heterogeneous crystallization and optical microscopy. The crystallization kinetics of an orthorhombic modification was linearly dependent in a logarithmic manner on the concentration of precipitants. The effects of polymorphs were observed in the crystallization kinetics. Lattice defects in lysozyme crystals were examined with laser scattering tomography and etching technique. The defects of point type were concentratedly distributed closer to the growing surfaces and growth sectors were observed. Heterogeneous crystallization on glass and polymer substrates was tried to selectively grow single crystals.Crystallization of three proteins was newly challenged : toxin protein yielded in bacteria, vegetable cell-producing protein and lectin produced from algae. Pure samples of about 1 0 mg yield of each substance was obtained from raw materials, and subjected to crystallization using vapor diffusion method. However, amorphous solids have so far been obtained. Further trials are needed for these substances.