Virus structure with cryo-EM

I study the structure and function of macromolecular complexes, such as virus capsids, using cryo-electron microscopy and combine this with subunit atomic models to extend interpretation into details of the protein folds and interfaces. Systems currently being studied include herpesviruses and dsDNA bacteriophages such as HK97, SPO1, T5 and others. These tailed phages have important structural similarities with each other and also with animal viruses such as herpesvirus, suggesting that there may be a long evolutionary connection between them. The dynamic aspects of the virus lifecycle – assembly, DNA packaging, infection and DNA delivery – are better suited to cryoEM study than crystallography. Achievable resolutions for icosahedral capsids are typically between 10-20Å, but new procedures such as automated data collection and high-speed data analysis are extending this to near atomic resolution in some cases. Lower symmetry structures, such as entire virus or phage particles, require more data and although resolutions are generally lower, these structures are rich in biology and improvements are also accruing from methodological advances. Ultimately, we aim to characterize the structural and functional repertoire of a virus throughout its lifecycle, which will have benefits in understanding protein-protein and protein-DNA interactions as well as the evolution of protein structure./This work will also lead to the development of new targets for interfering with viral infection and replication, and to technological applications.

 [PubMed search]


1989, Massey University, New Zealand

Postdoctoral Training

National Institutes of Health, NIAMS, Lab of Structural Biology Research

Department of Structural Biology
University of Pittsburgh
BST3; room 2047
3501 Fifth Ave
Pittsburgh, PA 15260

Phone: (412) 383-9847
Fax: (412) 648-8998


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