High pressure protein crystal structure analysis

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In order to elucidate the mechanism of pressure adaptation of proteins, we have developed structural studies of proteins by a high-pressure protein crystallography method using a diamond-anvil cell. IPMDH from the deep-sea bacterium Shewanella benthica DB21MT-2 is more tolerant towards HP stress than its counterpart from the land bacterium S. oneidensis MR-1, even though these two enzymes share 85% amino-acid identity. Crystal structures of IPMDH have been determined at about 2 A resolution under pressures ranging from 0. 1 to 650 MPa. Penetration of water molecules into IPMDH is observed at high-pressure, and relationship of the structure and pressure resistance has been elucidated.