Abstract
Our current understanding of the crystallization of globular proteins is reviewed. This includes protein growth mechanisms and kinetics, and recent results on nonsteady growth kinetics, morphological stability, impurity effects, striation formation, nonuniform precipitant repartitioning, as well as lattice strain and dislocations, that were mostly obtained for tetragonal hen-egg-white lysozyme. Furthermore, observations that indicate some interplay between solution flow conditions, growth kinetics and the resulting structural perfection are summarized. Recommendations for future research concern protein purification, protein-precipitant-solvent interactions, and the coupling between bulk transport and interface kinetics, together with well-characterized correlations between growth conditions and X-ray diffraction resolution.
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