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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review

Cryoelectron Microscopy

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Disease relevance of Cryoelectron Microscopy


High impact information on Cryoelectron Microscopy


Chemical compound and disease context of Cryoelectron Microscopy


Biological context of Cryoelectron Microscopy

  • Here we analyse three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states, and show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S subunit relative to the large 50S subunit [12].
  • A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis [13].
  • The cryo-electron microscopy reconstructions of echovirus 7 complexed with DAF show that the DAF-binding regions are located close to the icosahedral twofold axes, in contrast to other enterovirus complexes where the viral canyon is the receptor binding site [14].
  • The structure of the lipoplex formed from DNA and the sugar-based cationic gemini surfactant 1, which exhibits excellent transfection efficiency, has been investigated in the pH range 8.8-3.0 utilizing small-angle X-ray scattering (SAXS) and cryo-electron microscopy (cryo-TEM) [15].
  • Some TM proteins yield more easily to structure determination using cryo electron microscopy (cryo-EM), though this technique most often results in lower resolution structures, precluding an unambiguous assignment of TM amino acid sequences to the helices seen in the structure [16].

Anatomical context of Cryoelectron Microscopy


Associations of Cryoelectron Microscopy with chemical compounds


Gene context of Cryoelectron Microscopy


Analytical, diagnostic and therapeutic context of Cryoelectron Microscopy


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  2. Visualization of elongation factor Tu on the Escherichia coli ribosome. Stark, H., Rodnina, M.V., Rinke-Appel, J., Brimacombe, R., Wintermeyer, W., van Heel, M. Nature (1997) [Pubmed]
  3. Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Prasad, B.V., Burns, J.W., Marietta, E., Estes, M.K., Chiu, W. Nature (1990) [Pubmed]
  4. Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. Yeager, M., Berriman, J.A., Baker, T.S., Bellamy, A.R. EMBO J. (1994) [Pubmed]
  5. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Heymann, J.B., Cheng, N., Newcomb, W.W., Trus, B.L., Brown, J.C., Steven, A.C. Nat. Struct. Biol. (2003) [Pubmed]
  6. Cellular and molecular biology of the aquaporin water channels. Borgnia, M., Nielsen, S., Engel, A., Agre, P. Annu. Rev. Biochem. (1999) [Pubmed]
  7. Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Pokidysheva, E., Zhang, Y., Battisti, A.J., Bator-Kelly, C.M., Chipman, P.R., Xiao, C., Gregorio, G.G., Hendrickson, W.A., Kuhn, R.J., Rossmann, M.G. Cell (2006) [Pubmed]
  8. Structure of the human transferrin receptor-transferrin complex. Cheng, Y., Zak, O., Aisen, P., Harrison, S.C., Walz, T. Cell (2004) [Pubmed]
  9. Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae. Gilbert, R.J., Jiménez, J.L., Chen, S., Tickle, I.J., Rossjohn, J., Parker, M., Andrew, P.W., Saibil, H.R. Cell (1999) [Pubmed]
  10. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Roseman, A.M., Chen, S., White, H., Braig, K., Saibil, H.R. Cell (1996) [Pubmed]
  11. The organization of the spike complex of Semliki Forest virus. Vénien-Bryan, C., Fuller, S.D. J. Mol. Biol. (1994) [Pubmed]
  12. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Frank, J., Agrawal, R.K. Nature (2000) [Pubmed]
  13. Structure of the actin-myosin complex and its implications for muscle contraction. Rayment, I., Holden, H.M., Whittaker, M., Yohn, C.B., Lorenz, M., Holmes, K.C., Milligan, R.A. Science (1993) [Pubmed]
  14. Structure of decay-accelerating factor bound to echovirus 7: a virus-receptor complex. He, Y., Lin, F., Chipman, P.R., Bator, C.M., Baker, T.S., Shoham, M., Kuhn, R.J., Medof, M.E., Rossmann, M.G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  15. Transfection mediated by gemini surfactants: engineered escape from the endosomal compartment. Bell, P.C., Bergsma, M., Dolbnya, I.P., Bras, W., Stuart, M.C., Rowan, A.E., Feiters, M.C., Engberts, J.B. J. Am. Chem. Soc. (2003) [Pubmed]
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  17. Structures of kinesin and kinesin-microtubule interactions. Mandelkow, E., Hoenger, A. Curr. Opin. Cell Biol. (1999) [Pubmed]
  18. Evidence for cleft closure in actomyosin upon ADP release. Volkmann, N., Hanein, D., Ouyang, G., Trybus, K.M., DeRosier, D.J., Lowey, S. Nat. Struct. Biol. (2000) [Pubmed]
  19. Expression and subcellular localization of NRAMP1 in human neutrophil granules. Canonne-Hergaux, F., Calafat, J., Richer, E., Cellier, M., Grinstein, S., Borregaard, N., Gros, P. Blood (2002) [Pubmed]
  20. Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: role of the bound nucleotide in the structure of F-actin. Lepault, J., Ranck, J.L., Erk, I., Carlier, M.F. J. Struct. Biol. (1994) [Pubmed]
  21. The projection structure of microsomal glutathione transferase. Hebert, H., Schmidt-Krey, I., Morgenstern, R. EMBO J. (1995) [Pubmed]
  22. Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia coli at 6 A resolution. Gohlke, U., Warne, A., Saraste, M. EMBO J. (1997) [Pubmed]
  23. Evidence for a conformational change in actin induced by fimbrin (N375) binding. Hanein, D., Matsudaira, P., DeRosier, D.J. J. Cell Biol. (1997) [Pubmed]
  24. A novel immunogold cryoelectron microscopic approach to investigate the structure of the intracellular and extracellular forms of vaccinia virus. Roos, N., Cyrklaff, M., Cudmore, S., Blasco, R., Krijnse-Locker, J., Griffiths, G. EMBO J. (1996) [Pubmed]
  25. Structure of a human rhinovirus complexed with its receptor molecule. Olson, N.H., Kolatkar, P.R., Oliveira, M.A., Cheng, R.H., Greve, J.M., McClelland, A., Baker, T.S., Rossmann, M.G. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  26. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. Shorter, J., Watson, R., Giannakou, M.E., Clarke, M., Warren, G., Barr, F.A. EMBO J. (1999) [Pubmed]
  27. A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy. Rockel, B., Peters, J., Kühlmorgen, B., Glaeser, R.M., Baumeister, W. EMBO J. (2002) [Pubmed]
  28. The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Bella, J., Kolatkar, P.R., Marlor, C.W., Greve, J.M., Rossmann, M.G. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  29. Cryoelectron microscopy imaging of recombinant and tissue derived vaults: localization of the MVP N termini and VPARP. Mikyas, Y., Makabi, M., Raval-Fernandes, S., Harrington, L., Kickhoefer, V.A., Rome, L.H., Stewart, P.L. J. Mol. Biol. (2004) [Pubmed]
  30. Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). Rivera-Calzada, A., Maman, J.D., Maman, J.P., Spagnolo, L., Pearl, L.H., Llorca, O. Structure (Camb.) (2005) [Pubmed]
  31. Bacterial Na(+)-ATP synthase has an undecameric rotor. Stahlberg, H., Müller, D.J., Suda, K., Fotiadis, D., Engel, A., Meier, T., Matthey, U., Dimroth, P. EMBO Rep. (2001) [Pubmed]
  32. Efficient neutralization of foot-and-mouth disease virus by monovalent antibody binding. Verdaguer, N., Fita, I., Domingo, E., Mateu, M.G. J. Virol. (1997) [Pubmed]
  33. Coiled-coil packing in spermine-induced tropomyosin crystals. A comparative study of three forms. Xie, X., Rao, S., Walian, P., Hatch, V., Phillips, G.N., Cohen, C. J. Mol. Biol. (1994) [Pubmed]
  34. Structural characterisation of islet amyloid polypeptide fibrils. Sumner Makin, O., Serpell, L.C. J. Mol. Biol. (2004) [Pubmed]
  35. Filaments of the Ure2p prion protein have a cross-beta core structure. Baxa, U., Cheng, N., Winkler, D.C., Chiu, T.K., Davies, D.R., Sharma, D., Inouye, H., Kirschner, D.A., Wickner, R.B., Steven, A.C. J. Struct. Biol. (2005) [Pubmed]
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