Nature of impurities during protein crystallization
Lysozyme crystal growth was studied using reagents of different purity of three trademarks— Seikagaku Corporation (sixfold recrystallized lysozyme), Sigma-Aldrich (threefold recrystallized lysozyme), and Hampton Research (threefold recrystallized lysozyme). Solutions of these reagents were investigated by small-angle X-ray scattering, dynamic light scattering (DLS), ultracentrifugation, and electrophoresis. It was found that crystal-growth and oligomerization processes are more intense in solutions of the reagent of higher purity. The dependences of the fraction of lysozyme oligomers on the supersaturation and purity of the solution are analyzed.
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- 3.A. McPherson, Crystallization of Biological Macromolecules (Cold Spring Harbor Laboratory Press).Google Scholar
- 4.B. R. Thomas, P. G. Vekilov, and F. Rosenberger, Acta Crystallogr. 52, 776 (1996).Google Scholar
- 26.W. Brown, Dynamic Light Scattering: the Method and Some Applications (Clarendon, Oxford, 1993).Google Scholar