John Rubinstein Associate Professor

B.Sc., University of Guelph, 1998
Ph.D., University of Cambridge (MRC), 2002

Molecular Structure and Function Program
Hospital for Sick Children, Research Institute, 686 Bay Street
Room 20-9705

Electron cryomicroscopy of macromolecular assemblies

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Research Interests

  • Structural biology and electron cryomicroscopy
  • Structure and function of macromolecular assemblies
  • Membrane protein complexes
  • Bioenergetics

Research Synopsis

Electron cryomicroscopy (cryo-EM) of macromolecular assemblies has become an important technique in structural biology. The method allows biologists to bridge the resolution gap between images of cells from light microscopy and conventional electron microscopy and the high-resolution information from X-ray crystallography and NMR spectroscopy.

Our group uses cryo-EM to answer questions of fundamental importance to biochemistry and cell biology, and of significance to biomedical research. We are pursuing the structural analysis of membrane protein complexes, such as ATP synthases and vacuolar-type ATPases, with on-going studies related to the virulence of pathogenic bacteria. In addition to cryo-EM and image analysis, our group uses modern methods from biochemistry and molecular genetics to study these topics. Many of our projects involve close collaborations with biochemists, biophysicists, cell biologists, microbiologists, and clinician scientists.

For more details about our group's research, please see our laboratory home page.


Selected Publications

For a complete list of publications, please use [PubMed]

Lau WCY, Rubinstein JL (2011). Sub-nanometer resolution structure of the intact T. thermophilus H + -driven ATP synthase. Nature In Press.

Baker LA, Rubinstein JL (2011). Edged Watershed Segmentation: A semi-interactive algorithm for segmentation of low-resolution maps from electron cryomicroscopy . Journal of Structural Biology 176 , 127-32.

Lau WCY, Rubinstein JL (2010). Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V O motor. Proceedings of the National Academy of Sciences ( USA ) 107, 1367-72. (Selected by Faculty of 1000)

Baker LA, Smith EA, Bueler SA, Rubinstein JL. (2010). The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals. Journal of Structural Biology 169, 431-437.

Baker LA, Rubinstein JL (2010). Radiation damage in cryo-EM. Methods in Enzymology 481, 373-389.

Bueler SA, Rubinstein JL. (2008). Location of subunit d in the peripheral stalk of the ATP synthase from Saccharomyces cerevisiae. Biochemistry 47, 11804-11810.

Lau WCY, Baker LA, Rubinstein JL. (2008). Cryo-EM structure of the yeast ATP synthase. Journal of Molecular Biology 382, 1256-64.

Baker LA, Rubinstein JL. (2008) Angle determination for side views in single particle electron microscopy. Journal of Structural Biology 162, 260-270.

Rubinstein JL. (2007). Structural analysis of membrane protein complexes by single particle electron microscopy. Methods 41, 409 - 416.


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