Janet Smith

Our Research

Form determines function in biology, even at the level of individual molecules. The understanding of biological function derived from three-dimensional structures of key proteins is one of the most stunning outcomes of the molecular revolution in biology. The overall goal of our research is to understand biological function at the molecular level through knowledge of protein three-dimensional structure.

X-ray crystallography is the experimental method we use to determine protein structures; we have contributed to the development of new methods for rapid structure determination so that knowledge of key protein structures influences the study of biological problems early rather than retrospectively.

About Janet Smith

  • X-ray crystallography
  • Viruses and infectious disease
  • Drug discovery

Janet Smith focuses on understanding the complexity of protein structure and function using X-ray crystallography as a three-dimensional tool. Part of her research is in examining the structures of infectious pathogens including the RNA viruses that cause West Nile disease, yellow fever, and dengue hemorrhagic fever. She is the Director of the Center for Structural Biology.

JanetSmith [at] umich.edu

Highlight: Phleboviruses

The Smith lab found how a particular type of virus, the phlebovirus, hides and protects its genetic information from the immune system. It's the first picture of a potential drug target for the virus family, which attacks humans and animals via insect bites. Human cases of phleboviruses are on the rise, and some have been fatal, but there are no antivirals or immunizations.

The work was published in PNAS in October 2012.

Recent Publications

Efficient merging of data from multiple samples for determination of anomalous substructure. D. L. Akey, T. C. Terwilliger and J. L. Smith. Acta Crystallogr in press.

Can I solve my structure by SAD phasing? Anomalous signal in SAD phasing. T. C. Terwilliger, G. Bunkóczi, L.-W. Hung, P. H. Zwart, J. L. Smith, D. Akey and P. D. Adams. Acta Crystallogr in press.

Structural basis for cyclopropanation by a unique enoyl-acyl carrier protein reductase. D. Khare, W. A. Hale, A. Tripathi, L. Gu, D. H. Sherman, W. H. Gerwick, K. Håkansson and J. L. Smith (2015) Structure 23,2212-2223. PMC4670573.