Janet Smith's research focuses on understanding biological processes through knowledge of the structures of key protein molecules. She has made major contributions to the understanding of catalysis and regulation in glutamine amidotransferases and phosphoribosyltransferases by solving and interpreting crystal structures of several enzymes of each type. She has solved crystal structures of photosynthetic proteins, leading to a new understanding of their function. She has also contributed to the development of methods for rapid determination of protein crystal structures, particularly using synchrotron X-ray sources.
A native of Pennsylvania, Smith studied chemistry as a National Merit Scholar at Indiana University of Pennsylvania (B.S., 1973). Finding biochemistry to be the most stimulating area of chemistry, she continued her study in that field at the University of Wisconsin-Madison (Ph.D., 1978) where she was convinced of the importance of structure in biology by her research advisor M. Sundaralingam.
After her thesis research on crystal structures of protein synthesis inhibitors, Smith pursued a growing interest in protein structure by joining Wayne Hendrickson at the Naval Research Laboratory as a National Research Council Research Fellow. Following this postdoctoral work, she held positions as associate research scientist in Hendrickson lab and as associate research scientist at the Howard Hughes Medical Institute, both at Columbia University.
Smith established a research program in structural biology at Purdue in 1987, where she remained as a professor of biological sciences until moving to the LSI. She has been a visiting scientist at the European Molecular Biology Laboratory and the European Synchrotron Radiation Facility in Grenoble, France, and a lecturer at numerous international schools on structural biology and synchrotron radiation. She is also a frequent advisor to synchrotron radiation facilities and synchrotron structural biology labs both in the U.S. and abroad.
