Text Box:  Opportunities in the Department of Structural Biology
at the University of Pittsburgh School of Medicine

 

Positions in Cryo-electron Microscopy

The University of Pittsburgh School of Medicine has recently established a new Department of Structural Biology with state-of-the-art facilities in NMR, X-ray crystallography, cryo-electron microscopy as well as extensive biochemical and biophysical instrumentation. The Department is housed in the new Biomedical Science Tower-3, adjacent to existing departments in the School of Medicine and the University of Pittsburgh. We are establishing a program of exciting and high-quality research projects that are supported by our extensive technical resources including several NMR instruments ranging in field strength from 14.1 to 21.1 Tesla, two FR-E X-ray generators with four detectors including CCD and image plates, and FEI electron microscopes. Departmental resources include molecular biology and protein chemistry Cores in addition to extensive genomic and proteomics capabilities within the Medical School and the University of Pittsburgh. Both physical proximity and scientific affinities between the Medical School, the University, and Carnegie Mellon University extends the already expansive scope of research being conducted at Pittsburgh. The city of Pittsburgh consistently ranks among the “Best Places to Live in America” and is one of the nation’s top 25 arts destinations. The region is home to the Carnegie Museum of Art, Andy Warhol Museum and Pittsburgh Symphony Orchestra.

Cryo-electron microscopy is the focus of two independent groups led by Drs. James Conway and Peijun Zhang, and the facility is generously equipped with the latest in hardware, including three FEI Tecnai electron microscopes: Polara and T20F, both with field emission guns and Gatan 4k CCD cameras, and a T12 with LaB6 source. Additional equipment includes a Vitrobot and ancillary equipment for routine negative-stain EM and cryo-EM, and a darkroom. The biological focus is on cryo-EM imaging and three-dimensional reconstruction of protein assemblies such as virus capsids and endocytotic machinery, with the goal of under­standing function at the protein subunit and complex levels, and the relationship between function and structure. Methods include high-resolution “single-particle” structure analyses and electron tomography, which are under continual development.

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