STUDIES OF CRYO-COOLING AND CATALYTIC MECHANISM IN E COLI BETA-GALACTOSIDASE

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Three experiments are described involving E. coli beta-galactosidase designed to address three broadly related topics. First is to improve our basic knowledge about cryocooling by understanding the cryocooling induced repacking in crystals of beta-galactosidase. Second is to understand how packing forces modulate enzyme activity by characterizing differences in ligand binding to separate subunits in an asymmetric unit. And third is to understand the role of a conformational switch in the activity of beta-galactosidase and how packing forces affect this switch. Each experiment is straightforward in principle, but technically demanding given the large size of the unit cell. Structures of variants and complexes will be determined up to 1.1 ¿¿resolution.