STRUCTURAL INVESTIGATIONS ON THE ETOH BMC OF E COLI, ENGINEERED ALLOSTERIC PROT

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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. Beam time is requested for three ongoing projects regarding 1) the structure and function of the bacterial ethanolamine ammonia lyase microcompartment of, E. coli 2) the engineering of allosteric functions into proteins and 3) the structure and function of the solvent-stable cholesterol oxidase from Chromobacterium sp. DS-1. The preliminary work on all research directions has resulted in crystals or crystalline material that requires high-energy x-ray sources. In all cases, we request access to monochromatic beamlines as most crystallographic structures are likely to be solved by molecular replacement. With regards to the work on the bacterial ethanolamine microcompartment, current work on the EutQ protein (see below) may require access to MAD beamlines.