Overview
Electron cryomicroscopy (cryo-EM) is an emerging structure determination technique for solving structures of large macromolecular assemblies. Cryo-EM does not require crystalline order for the studied object. This unique capability makes cryo-EM extremely valuable in imaging and solving the structures and the dynamics of macromolecular machines.The research in this lab focuses on the development of cryo-EM techniques to push for near atomic resolution single particle 3-D reconstruction, to improve the tomographic three-dimensional reconstruction, and to improve the cryo-EM project throughput to eventually transform the cryo-EM technique into a common laboratory tool for functional studies of biological systems. To achieve these goals, our research involves development of new image processing algorithms, high performance computing, data collection automation and reliable sample freezing. These techniques are applied to study the biological systems including enveloped viruses (alphavirus and flavivirus) and bacteriophages (T7, Epsilon15).
Equipments
Exellent equipments are available just down the hall way that are managed by the Biological Electron Microscopy Facility.Two FEI microscopes (CM300F and CM200F) are both equiped with field emission gun, 4kx4k CCD camera and liquid nitrogen temperature holders. These two microscopes are generating large volume of high resolution images that allowed numerous high impact discoveries and publications.
Two older microscopes (EM420 and EM410) are also available for routine initial feasibility studies, sample screening, and user training.
Journal Covers
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Liu, X., Jiang, W., Jakana, J. and Chiu, W. 2007. Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a multi-path simulated annealing optimization algorithm. J. Struct. Biol. 160(1):11-27 | PubMed | |
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Pope, W. H., Weigele, P.R., Chang, J., Pedulla, M.L., Ford, M.E., Houtz, J.M., Jiang, W., Chiu, W., Hatfull, G.F., Hendrix, R.W. and King, J. 2007. Genome sequence, structural proteins, and capsid organization of the cyanophage syn5: a "horned" bacteriophage of marine synechococcus. J. Mol. Biol. 368(4):966-81 | PubMed | |
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Chiu W, Chen D, Jakana J, Chang J, Jiang W, Ludtke SJ, Baker ML. 2006. Visualization of biological nano-machines at subnanometer resolutions. JEOL News 41(1):12-17 | JEOL News | |
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Jiang, W., Chang, J., Jakana, J., Weigele, P., King, J., and Chiu, W. 2006. Structure of complete Epsilon15 phage reveals organization of condensed DNA and DNA packaging/injection apparatus. Nature 439(7076):612-616 | PubMed | |
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Booth, C. R., Jiang, W., Baker, M. L., Zhou, Z. H., Ludtke, S. J., and Chiu, W. 2004. A 9 Å single particle peconstruction from CCD captured images on a 200kV electron cryomicroscope. J. Struct. Biol. 147:116-27 | PubMed | |
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Jiang, W., Li, Z., Zhang, Z., Baker, M. L., Prevelige, P. E., and Chiu, W. 2003. Coat protein fold and maturation transition of bacteriophage p22 seen at subnanometer resolutions. Nat. Struct. Biol. 10:131-135 | PubMed | |
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Chiu, W., Baker, M. L., Jiang, W., and Zhou, Z. H. 2002. Deriving folds of macromolecular complexes through electron cryomicroscopy and bioinformatics approaches. Curr. Opin. Struct. Biol. 12:263-269. | PubMed | |
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Zhou, Z. H., Baker, M. L., Jiang, W., Dougherty, M., Jakana, J., Dong, G., Lu, G., and Chiu, W. 2001. Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nat. Struct. Biol. 8:868-873. | PubMed | |
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Jiang, W., Baker, M. L., Ludtke, S. J., and Chiu, W. 2001. Bridging the information gap: Computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308:1033-1044 | PubMed | |