Dave Agard, PhD


Our research is focused on elucidating the mechanism of Hsp90 chaperone function and its role in human disease, microtubule nucleation & centrosome structure, and the structure and cell biology of phage-encoded tubulins. Accompanying this is an effort to develop new technologies for high-resolution cryoEM and fluorescence light microscopy.

Yifan Cheng, PhD


We are interested in studying the three-dimensional structures of macromolecular complexes: their structural architectures, the regulation of their function and the dynamic processes of their assembly and disassembly, by molecular electron microscopy (cryoEM). A full understanding of the biological functions/processes of any macromolecular complex requires structural information at a wide range of resolutions, including atomic details of its components, spatial arrangements of these components and interactions between them.

Daniel Southworth, PhD

Associate Professor

Our lab focuses on understanding molecular chaperone-driven protein quality control mechanisms that facilitate protein folding and cellular stress responses.  A protein must fold into a native state or a range of three-dimensional states in order to carry out biological functions, and must retain a certain degree of flexibility to accommodate various chemistries and binding events.