2006 年 33 巻 4 号 p. 240-
We studied the impurity effects of two impure proteins, fluorescent-labeled lysozyme and covalently-bonded dimmer of lysozyme, on the behavior of elementary growth steps of tetragonal lysozyme crystals. Two impure proteins gave the different supersaturation dependencies of the step velocities. To clarify the cause, we observed in situ the adsorption processes of these two impure proteins on the surface of the lysozyme crystals, and concluded that the different adsorption sites of the impurities resulted in the different supersaturation dependencies of the step velocities.