Bi-cheng (B.-C.) Wang Professor of Biochemistry & Molecular Biology Eminent Scholar in Structural Biology (X-ray Crystallography) Professor Wang received a Ph.D. degree from the University of Arkansas in 1968 and continued research training through a postdoctoral position at the California Institute of Technology until 1970. He was then a research associate at the University of Pittsburgh, followed by several positions at the VA Medical Center in Pittsburgh and Professor of Crystallography and Biological Sciences at the University of Pittsburgh from 1986 through 1995. Using X-ray crystallography as a tool, our group is engaging in structure-function studies on a variety of relevant biological macromolecules: T7 RNA polymerase (T7 RNAP) and its DNA-RNA complexes. Our objective is to help understand the structure-function relationship of RNA polymerase at the atomic level. The crystal structure of T7 RNAP is being refined and extended to the highest resolution possible. Neurophysins (NPs) and their hormone complexes. NPs (22-kDa dimers) are carrier proteins for the hormone oxytocin and vasopressin. Bovine NP has been cocrystallized with oxytocin, vasopressin and with hormone-related peptides in eleven different crystal forms. In addition, our group is also studying the conformational dynamics of NPs by molecular dynamics simulations. Glutathione transferases (GST). GSTs (50-kDa dimers) are binding proteins that detoxify chemical carcinogens. Several related m-family rat GSTs and a-family human GST isozymes and their mutants have been crystallized and are under structural analyses. Augmentor of liver regeneration (ALR). ALR is a new hepatic growth factor for the generation of liver cells. Crystals of ALR have been grown and are under structural analysis. We are also interested in determining the structures of mutant proteins of ALR and ALR-antibody complexes. Aldehyde dehydrogenase (AlDH). AlDH (100-kDa dimers) plays a pivotal role in human alcohol metabolism as the major route through which ethanol-derived acetaldehyde is cleaved, via conversion to acetate. The structure of rat class 3 AlDH has recently been determined. Glutamine binding protein (GlnBP). GlnBP (26 kDa) is responsible for the first step in the active transport of L-Gln across the cytoplasmicmembrane. Ligand-free and ligand-bound GlnBPs have been crystallized in five different crystal forms. Other proteins which have been crystallized include the green fluorescent protein from jellyfish and an unusual hemoprotein capable of reversibly binding nitric oxide. Under crystallization trials are the L5 integrase (41 kDa), the HIV transactivation protein TAT (10 kDa) and a novel regulator protein in GTP cyclohydrolase. We are also collaborating with a number of local research groups in the structural studies of transcription factors, enzymes in lignin biosynthesis, oligosaccharides and oligosaccharide-receptor complexes. "The Crystal Structure of Bacteriophage T7 RNA Polymerase at 3.3 Å Resolution," R. Sousa, Y. J. Chung, J. P. Rose, and B. C. Wang, Nature. 1993, 364, 593-599. "Crystal Structure of the Neurophysin-Oxytocin Complex," J. P. Rose, C. K. Wu, C. H. Hsaio, E. Breslow and B. C. Wang, Nature Structural Biology 1996, 3, 163-169. E-mail contact: wang@bcl1.bmb.uga.edu Website: http://www.uga.edu/~biocryst