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Three-dimensional electron cryomicroscopy

Stansfield 1, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski Al, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite ME (1995) The products of the SUP45 (eRFl) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14 4365 373 Stansfield 1, Eurwilaichitr L, Akhmaloka, Tuite ME (1996) Depletion in the levels of the release factor eRFl causes a reduction in the efficiency of translation termination in yeast. Mol Microbiol 20 1135-1143 Stansfield 1, Kushnirov VV, Jones KM, Tuite ME (1997) A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae. Fur J Biochem 245 557-563 Stark H (2002) Three-dimensional electron cryomicroscopy of ribosomes. Curr Protein Pept Sci 3 79-91... [Pg.28]

Hirose, K., Lowe,J., Alonso, M., Cross, R. A., and Amos, L. A. (1999). Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes. Mol. Biol. CeU 10, 2063-2074. [Pg.340]

Akiba, T., Toyoshima, C., Matsunaga, T., Kawamoto, M., Kubota, T., Fukuyama, K., Namba, K., and Matsubara, H., 1996, Three-dimensional structure of bovine cytochrome bcl complex by electron cryomicroscopy and helical image reconstruction. Nature Struct. Biol. 3 553n561. [Pg.573]

Bottcher, B., Kiselev, N. A., Stel Mashchuk, V. Y., Perevozchikova, N. A., Borisov, A. V., and Crowther, R. A. (1997a). Three-dimensional structure of infectious bursal disease virus determined by electron cryomicroscopy. / Virol. 71, 325-330. [Pg.250]

Electron cryomicroscopy, 2, 94-101, 401-2 field depth/resolution graph for, 100 instrument choices in, 97-101 theoretical consideration of, 94-101 three dimensional reconstruction and, 101 Electron density maps, 42 Electron microscopy resolution (EM resolution), 45-46... [Pg.534]

Orlova EV, Sherman MB, Chiu W, Mowri H, Smith LC, Gotto AM. Jr. Three-dimensional structure of low density lipoproteins by electron cryomicroscopy. Proc. Natl. Acad. Sci. U.S.A. 1999 96 8420-8425. [Pg.392]

Nield J, Balsera M, de las Rivas J et al. Three-dimensional Electron Cryomicroscopy Study of the Extrinsic Domains of the Oxygen-evolving Complex from Spinach. J Biol Chem 2002 277 15006-15012. [Pg.29]

Fig. 28-3. Structure of an alphavirus. Shown is the three-dimensional reconstruction of Sindbis virus at 28 A resolution from computer-processed images taken by electron cryomicroscopy, (a) The original electron micrograph shows virus particles in vitreous ice. (b) The surface view of the virus shows details of the 80 trimeric spikes, which are arranged in a T=4 icosahedron. Each spike protrudes 50 A from the virion surface and is believed to be composed of three E1-E2 glycoprotein heterodimers, (c) The cross-sectional view shows the outer surface spikes (yellow) and the internal nucleocapsid (blue), composed of the capsid and viral RNA. The space between the spikes and the nucleocapsid would be occupied by the lipid envelope. The green arrows mark visible points of interaction between the nucleocapsid and trans-membranal tails of the glycoprotein spikes, (d) The reconstructed capsid also exhibits a T=4 icosahedral symmetry. Computer models Courtesy of Angel M. Paredes, Cell Research Institute and Department of Microbiology, The University of Texas at Austin, Austin, Tex. Similar but not identical versions of these computer models were published in Paredes AM, Brown DT, Rothnagel R, et al. Three-dimensional structure of a membrane-containing virus. Proc Natl Acad Sci USA. 1993 90 9095-9099. Fig. 28-3. Structure of an alphavirus. Shown is the three-dimensional reconstruction of Sindbis virus at 28 A resolution from computer-processed images taken by electron cryomicroscopy, (a) The original electron micrograph shows virus particles in vitreous ice. (b) The surface view of the virus shows details of the 80 trimeric spikes, which are arranged in a T=4 icosahedron. Each spike protrudes 50 A from the virion surface and is believed to be composed of three E1-E2 glycoprotein heterodimers, (c) The cross-sectional view shows the outer surface spikes (yellow) and the internal nucleocapsid (blue), composed of the capsid and viral RNA. The space between the spikes and the nucleocapsid would be occupied by the lipid envelope. The green arrows mark visible points of interaction between the nucleocapsid and trans-membranal tails of the glycoprotein spikes, (d) The reconstructed capsid also exhibits a T=4 icosahedral symmetry. Computer models Courtesy of Angel M. Paredes, Cell Research Institute and Department of Microbiology, The University of Texas at Austin, Austin, Tex. Similar but not identical versions of these computer models were published in Paredes AM, Brown DT, Rothnagel R, et al. Three-dimensional structure of a membrane-containing virus. Proc Natl Acad Sci USA. 1993 90 9095-9099.

See other pages where Three-dimensional electron cryomicroscopy is mentioned: [Pg.110]    [Pg.247]    [Pg.203]    [Pg.94]    [Pg.450]    [Pg.611]    [Pg.615]    [Pg.615]    [Pg.10]    [Pg.154]    [Pg.2472]   
See also in sourсe #XX -- [ Pg.615 ]

See also in sourсe #XX -- [ Pg.615 ]




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