Effect of Fibrinolytic Compound GDG on Crystal Structure of Lysozyme

Abstract

Lysozyme was extensively studied as a model of protein crystallization, we identified that 15 mg/ml lysozyme, 0.1 M sodium acetate buffer containing 5% (w/v) sodium chloride and 0.02% (w/v) sodium azide, pH 5.2, crystal nucleus were less and crystals could reach a certain size. Basic on GDG effected conformation of enzyme which enhancing the reciprocal activation of plasminogen and prourokinase via the elevation of intrinsic activity of prourokinase, we obtained the crystal of lysozyme added α-D-glucopyranoslydiacylglycerol (GDG), GDG: HEWL (c/c) = 2:1, 1:1, 1:2, performed the synchrotron radiation diffraction and collected the three dimensional structure data. It is showing that increased in number of crystal amount and decreased in volume of crystal size in crystallization of lysozyme accompanied by the concentration of GDG. It is not displayed effect on the main chain and most side chains of lysozyme in the presence of GDG in the electron density map.