Focused irradiation of femtosecond laser pulses can induce nucleation of various proteins at low supersaturation, where high quality protein crystals can be obtained. Recently we studied the nucleation mechanism by fast-imaging methods and found that the rapid shrinkage (microsecond-scale) of a laser-induced cavitation bubble creates a local high concentration of protein. Actually, the surface of cavitation bubbles is known to be a preferred region for protein adsorption. Hence, protein molecules adsorbed at the surface during the expansion will be then gathered to the center region by the rapid shrinking of cavitation bubbles. These results indicate the femtosecond laser technique is based on a fundamental crystallization parameter, concentration, and can work as a nucleation trigger of various materials. In this paper, we introduce our recent studies of the nucleation mechanism and the development of the technique for protein nucleation at lower supersaturation.
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