Protein is the basis of life.Using the X-ray diffraction technique to determine the three dimensional structure of proteins has a significant meaning to help understanding the life process and the guiding of the new drug design.Chicken egg white lysozyme has been extensively studied as a model of protein-crystal growth because of its stability, solubility and ease of crystallization.In this paper, by optimizing the crystallization condition of tetragonal lysozyme, 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, pH5.2, crystal nucleus were less and crystals could reach a certain size.We obtained the crystal oflysozyme added GDG, GDG∶ HEWL (c/c) =2∶ 1, 1 ∶ 1, 1 ∶ 2, performed the synchrotron radiation diffusion and collected the three dimensional structure data oflysozyme added GDG (GDG∶ HEWL (c/c) =1∶ 1).But the determination of the structure has not completed yet.We studied the influence of GDG on crystal structure of lysozyme, and that we would need to further investigate effect of GDG on crystal structure of fibrinolytic factors.