Abstract
Pressure is an attractive thermodynamic parameter. In this review, I present the great potentialities of high pressure for the promotion of studies on the enhancement of protein crystallization processes and correlation between functions and 3D structures of protein molecules. As a tool for enhancing the crystal growth, three of eight proteins show the decrease in its solubility under high pressure. Acceleration of growth and nucleation kinetics of glucose isomerase crystals occurred under high pressure. Step velocities under high pressure provided us direct information on activation volumes during incorporation processes of protein molecules at a kink site of crystals. Such activation volumes were negative in the case of glucose isomerase crystals. Precise discussion on the activation volume will be useful for understanding dehydration mechanisms during the incorporation processes. Usefulness of our standalone-type Be vessel for high-pressure protein crystallography was confirmed. With the vessel, precise high-pressure 3D structure analysis of protein crystals which are also grown under high pressure will be achieved.
