STRUCTURE BIOLOGY OF ENZYMES AND DNA-BINDING PROTEINS

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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. Data were collected for a variety of proteins at different stages of structure determination and exploitation. For tyrosine decarboxylase, heavy-atom derivative data were collected. This protein is a PLP-containing enzyme being studied as part of an ongoing project about protein stability and the structural basis of PLP catalysis. For chymotrypsin and aminopeptidase, ultra-high resolution data were collected as part of an ongoing project about the location of hydrogens in protein structures and the role of anisotropic motion in catalysis. For thiaminase, derivative data were collected in order to try to solve the structure of this cancer-related protein. Data were also collected on the C-terminal domain of the bacterial repressor DtxR with some putative bound peptides. A number of other crystals of projects getting underway were screened for diffraction.