메뉴 건너뛰기




Volumn 33, Issue , 2004, Pages 141-155

Three-dimensional electron microscopy at molecular resolution

Author keywords

Automation; Cryo electron microscopy; Electron tomography; Three dimensional imaging; Three dimensional reconstruction

Indexed keywords

PROTEIN;

EID: 3042548142     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.33.110502.140339     Document Type: Review
Times cited : (65)

References (111)
  • 1
    • 0142057237 scopus 로고    scopus 로고
    • An oscillating cryo-knife reduces cutting-induced deformation of vitreous ultrathin sections
    • Al-Amoudi A, Dubochet J, Gnaegi H, Lüthi W, Studer D. 2003. An oscillating cryo-knife reduces cutting-induced deformation of vitreous ultrathin sections. J. Microsc. 212:26-33
    • (2003) J. Microsc. , vol.212 , pp. 26-33
    • Al-Amoudi, A.1    Dubochet, J.2    Gnaegi, H.3    Lüthi, W.4    Studer, D.5
  • 2
    • 0026708845 scopus 로고
    • A 360 degrees single-axis tilt stage for the high-voltage electron microscope
    • Barnard DP, Turner JN, Frank J, McEwen BF. 1992. A 360 degrees single-axis tilt stage for the high-voltage electron microscope. J. Microsc. 167:39-48
    • (1992) J. Microsc. , vol.167 , pp. 39-48
    • Barnard, D.P.1    Turner, J.N.2    Frank, J.3    McEwen, B.F.4
  • 4
    • 0034687769 scopus 로고    scopus 로고
    • Toward detecting and identifying macromolecules in a cellular context: Template matching applied to electron tomograms
    • Böhm J, Frangakis AS, Hegerl R, Nickell S, Typke D, Baumeister W. 2000. Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms. Proc. Natl. Acad. Sci. USA 97:14245-50
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14245-14250
    • Böhm, J.1    Frangakis, A.S.2    Hegerl, R.3    Nickell, S.4    Typke, D.5    Baumeister, W.6
  • 5
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B, Wynne SA, Crowther RA. 1997. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386:88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 6
    • 0035783045 scopus 로고    scopus 로고
    • Automatic alignment of transmission electron microscope tilt series without fiducial markers
    • Brandt S, Heikkonen J, Engelhardt P. 2001. Automatic alignment of transmission electron microscope tilt series without fiducial markers. J. Struct. Biol. 136:201-13
    • (2001) J. Struct. Biol. , vol.136 , pp. 201-213
    • Brandt, S.1    Heikkonen, J.2    Engelhardt, P.3
  • 7
    • 0028206095 scopus 로고
    • Cryo automated electron tomography: Towards high-resolution reconstructions of plastic-embedded structures
    • Braunfeld MB, Koster AJ, Sedat JW, Agard DA. 1994. Cryo automated electron tomography: towards high-resolution reconstructions of plastic-embedded structures. J. Microsc. 174:75-84
    • (1994) J. Microsc. , vol.174 , pp. 75-84
    • Braunfeld, M.B.1    Koster, A.J.2    Sedat, J.W.3    Agard, D.A.4
  • 8
    • 0032807499 scopus 로고    scopus 로고
    • The BioImage Database Project: Organizing multidimensional biological images in an object-relational database
    • Carazo JM, Stelzer EH. 1999. The BioImage Database Project: organizing multidimensional biological images in an object-relational database. J. Struct. Biol. 125:97-102
    • (1999) J. Struct. Biol. , vol.125 , pp. 97-102
    • Carazo, J.M.1    Stelzer, E.H.2
  • 10
    • 0036297629 scopus 로고    scopus 로고
    • Multiresolution contour-based fitting of macromolecular structures
    • Chacón P, Wriggers W. 2002. Multiresolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317: 375-84
    • (2002) J. Mol. Biol. , vol.317 , pp. 375-384
    • Chacón, P.1    Wriggers, W.2
  • 11
    • 0035783170 scopus 로고    scopus 로고
    • Real space refinement of actomyosin structures from sectioned muscle
    • Chen LF, Blanc E, Chapman MS, Taylor KA. 2001. Real space refinement of actomyosin structures from sectioned muscle. J. Struct. Biol. 133:221-32
    • (2001) J. Struct. Biol. , vol.133 , pp. 221-232
    • Chen, L.F.1    Blanc, E.2    Chapman, M.S.3    Taylor, K.A.4
  • 12
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway JF, Cheng N, Zlotnick A, Wingfield PT, Stahl SJ, Steven AC. 1997. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 386:91-94
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 13
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther RA, Amos LA, Finch JT, De Rosier DJ, Klug A. 1970. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 226:421-25
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 14
    • 0000668797 scopus 로고
    • Reconstruction of 3-dimensional structures from electron micrographs
    • DeRosier D, Klug A. 1968. Reconstruction of 3-dimensional structures from electron micrographs. Nature 217:130-34
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.1    Klug, A.2
  • 16
    • 0033793451 scopus 로고    scopus 로고
    • CCD detectors in high-resolution biological electron microscopy
    • Faruqi AR, Subramaniam S. 2000. CCD detectors in high-resolution biological electron microscopy. Q. Rev. Biophys. 33:1-27
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 1-27
    • Faruqi, A.R.1    Subramaniam, S.2
  • 19
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis AS, Hegerl R. 2001. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 135:239-50
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 21
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank J. 2002. Single-particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biomol. Struct. 31:303-19
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 303-319
    • Frank, J.1
  • 22
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey TG, Mannella CA. 2000. The internal structure of mitochondria. Trends Biochem. Sci. 25:319-24
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 23
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi Y. 1998. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 35:25-80
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 24
    • 0037229780 scopus 로고    scopus 로고
    • Depositing electron microscopy maps
    • Fuller SD. 2003. Depositing electron microscopy maps. Structure 11:11-12
    • (2003) Structure , vol.11 , pp. 11-12
    • Fuller, S.D.1
  • 27
    • 0037306721 scopus 로고    scopus 로고
    • Protein complexes and proteome organization from yeast to man
    • Gavin AC, Superti-Furga G. 2003. Protein complexes and proteome organization from yeast to man. Curr. Opin. Chem. Biol. 7:21-27
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 21-27
    • Gavin, A.C.1    Superti-Furga, G.2
  • 29
    • 0015106320 scopus 로고
    • Limitations to significant information in biological electron microscopy as a result of radiation damage
    • Glaeser RM. 1971. Limitations to significant information in biological electron microscopy as a result of radiation damage. J. Ultrastruct. Res. 36:466-82
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 466-482
    • Glaeser, R.M.1
  • 30
    • 0033377941 scopus 로고    scopus 로고
    • Review: Electron crystallography: Present excitement, a nod to the past, anticipating the future
    • Glaeser RM. 1999. Review: electron crystallography: present excitement, a nod to the past, anticipating the future. J. Struct. Biol. 128:3-14
    • (1999) J. Struct. Biol. , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 31
    • 0343582773 scopus 로고
    • Low temperature electron microscopy: Radiation damage in crystalline biological materials
    • Glaeser RM, Cosslett VE, Valdre U. 1971. Low temperature electron microscopy: radiation damage in crystalline biological materials. J. Microsc. 12:133-38
    • (1971) J. Microsc. , vol.12 , pp. 133-138
    • Glaeser, R.M.1    Cosslett, V.E.2    Valdre, U.3
  • 32
    • 0038670209 scopus 로고    scopus 로고
    • Molecular architecture of the multiprotein splicing factor SF3b
    • Golas MM, Sander B, Will CL, Lührmann R, Stark H. 2003. Molecular architecture of the multiprotein splicing factor SF3b. Science 300:980-84
    • (2003) Science , vol.300 , pp. 980-984
    • Golas, M.M.1    Sander, B.2    Will, C.L.3    Lührmann, R.4    Stark, H.5
  • 34
    • 0037438344 scopus 로고    scopus 로고
    • Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: Implications of crowding
    • Grünewald K, Medalia O, Gross A, Steven AC, Baumeister W. 2003. Prospects of electron cryotomography to visualize macromolecular complexes inside cellular compartments: implications of crowding. Biophys. Chem. 100:577-91
    • (2003) Biophys. Chem. , vol.100 , pp. 577-591
    • Grünewald, K.1    Medalia, O.2    Gross, A.3    Steven, A.C.4    Baumeister, W.5
  • 35
    • 0035945556 scopus 로고    scopus 로고
    • The architecture of active zone material at the frog's neuromuscular junction
    • Harlow ML, Ress D, Stoschek A, Marshall RM, McMahan UJ. 2001. The architecture of active zone material at the frog's neuromuscular junction. Nature 409:479-84
    • (2001) Nature , vol.409 , pp. 479-484
    • Harlow, M.L.1    Ress, D.2    Stoschek, A.3    Marshall, R.M.4    McMahan, U.J.5
  • 36
    • 0014433959 scopus 로고
    • Electron microscopy of unstained biological material: The polytropic montage
    • Hart RG. 1968. Electron microscopy of unstained biological material: the polytropic montage. Science 159:1464-67
    • (1968) Science , vol.159 , pp. 1464-1467
    • Hart, R.G.1
  • 37
    • 3943108224 scopus 로고
    • Influence of electron noise on three-dimensional image reconstruction
    • Hegerl R, Hoppe W. 1976. Influence of electron noise on three-dimensional image reconstruction. Z. Naturforsch. 31a:1717-21
    • (1976) Z. Naturforsch. , vol.31 A , pp. 1717-1721
    • Hegerl, R.1    Hoppe, W.2
  • 38
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson R. 1995. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28:171-93
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 39
  • 40
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryoelectron microscopy
    • Heymann JB, Cheng N, Newcomb WW, Trus BL, Brown JC, Steven AC. 2003. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryoelectron microscopy. Nat. Struct. Biol. 10:334-41
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 41
    • 0016192256 scopus 로고
    • Towards three-dimensional "electron microscopy" at atomic resolution
    • Hoppe W. 1974. Towards three-dimensional "electron microscopy" at atomic resolution. Naturwissenschaften 61:239-49
    • (1974) Naturwissenschaften , vol.61 , pp. 239-249
    • Hoppe, W.1
  • 42
    • 0016327614 scopus 로고
    • Three-dimensional reconstruction of individual negatively stained yeast fatty-acid synthetase molecules from tilt series in the electron microscope
    • Hoppe W, Gaßmann J, Hunsmann N, Schramm HJ, Sturm M. 1974. Three-dimensional reconstruction of individual negatively stained yeast fatty-acid synthetase molecules from tilt series in the electron microscope. Hoppe Seyler's Z. Physiol. Chem. 355:1483-87
    • (1974) Hoppe Seyler's Z. Physiol. Chem. , vol.355 , pp. 1483-1487
    • Hoppe, W.1    Gaßmann, J.2    Hunsmann, N.3    Schramm, H.J.4    Sturm, M.5
  • 43
    • 0016840484 scopus 로고
    • Comments on the paper "Relevance of three-dimensional reconstructions of stain distributions for structural analysis of biomolecules."
    • Hoppe W, Gaßmann J, Hunsmann N, Schramm HJ, Sturm M. 1975. Comments on the paper "Relevance of three-dimensional reconstructions of stain distributions for structural analysis of biomolecules." Hoppe Seyler's Z. Physiol. Chem. 356:1317-20
    • (1975) Hoppe Seyler's Z. Physiol. Chem. , vol.356 , pp. 1317-1320
    • Hoppe, W.1    Gaßmann, J.2    Hunsmann, N.3    Schramm, H.J.4    Sturm, M.5
  • 44
    • 0014303156 scopus 로고
    • Protein crystal structure analysis with electron radiation
    • Transl. From German
    • Hoppe W, Langer R, Knesch G, Poppe C. 1968. Protein crystal structure analysis with electron radiation. Transl. Naturwissenschaften 55:333-36 (From German)
    • (1968) Naturwissenschaften , vol.55 , pp. 333-336
    • Hoppe, W.1    Langer, R.2    Knesch, G.3    Poppe, C.4
  • 45
    • 0036410825 scopus 로고    scopus 로고
    • Electron tomographic analysis of frozen-hydrated tissue sections
    • Hsieh CE, Marko M, Frank J, Mannella CA. 2002. Electron tomographic analysis of frozen-hydrated tissue sections. J. Struct. Biol. 138:63-73
    • (2002) J. Struct. Biol. , vol.138 , pp. 63-73
    • Hsieh, C.E.1    Marko, M.2    Frank, J.3    Mannella, C.A.4
  • 46
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • 45a. Jiang W, Li Z, Zhang Z, Baker ML, Prevelige PE, Chiu W. 2003. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat. Struct. Biol. 10:131-35
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige, P.E.5    Chiu, W.6
  • 47
    • 0020633272 scopus 로고
    • Three-dimensional reconstruction and averaging of 30 S ribosomal subunits of Escherichia coli from electron micrographs
    • Knauer V, Hegerl R, Hoppe W. 1983. Three-dimensional reconstruction and averaging of 30 S ribosomal subunits of Escherichia coli from electron micrographs. J. Mol. Biol. 163:409-30
    • (1983) J. Mol. Biol. , vol.163 , pp. 409-430
    • Knauer, V.1    Hegerl, R.2    Hoppe, W.3
  • 50
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71-76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 51
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments
    • Ladinsky MS, Wu CC, McIntosh S, McIntosh JR, Howell KE. 2002. Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments. Mol. Biol. Cell 13:2810-25
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.C.2    McIntosh, S.3    McIntosh, J.R.4    Howell, K.E.5
  • 52
    • 0037392232 scopus 로고    scopus 로고
    • Detecting single atoms of calcium and iron in biological structures by electron energy-loss spectrum-imaging
    • Leapman RD. 2003. Detecting single atoms of calcium and iron in biological structures by electron energy-loss spectrum-imaging. J. Microsc. 210:5-15
    • (2003) J. Microsc. , vol.210 , pp. 5-15
    • Leapman, R.D.1
  • 53
    • 0033007093 scopus 로고    scopus 로고
    • Towards single atom analysis of biological structures
    • Leapman RD, Rizzo NW. 1999. Towards single atom analysis of biological structures. Ultramicroscopy 78:251-68
    • (1999) Ultramicroscopy , vol.78 , pp. 251-268
    • Leapman, R.D.1    Rizzo, N.W.2
  • 54
    • 0037079068 scopus 로고    scopus 로고
    • Depolarization redistributes synaptic membrane and creates a gradient of vesicles on the synaptic body at a ribbon synapse
    • Lenzi D, Crum J, Ellisman MH, Roberts WM. 2002. Depolarization redistributes synaptic membrane and creates a gradient of vesicles on the synaptic body at a ribbon synapse. Neuron 36:649-59
    • (2002) Neuron , vol.36 , pp. 649-659
    • Lenzi, D.1    Crum, J.2    Ellisman, M.H.3    Roberts, W.M.4
  • 55
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database
    • Liang Y, Ke EY, Zhou ZH. 2002. IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database. J. Struct. Biol. 137:292-304
    • (2002) J. Struct. Biol. , vol.137 , pp. 292-304
    • Liang, Y.1    Ke, E.Y.2    Zhou, Z.H.3
  • 56
    • 0029311291 scopus 로고
    • A marker-free alignment method for electron tomography
    • Liu Y, Penczek PA, McEwen BF, Frank J. 1995. A marker-free alignment method for electron tomography. Ultramicroscopy 58:393-402
    • (1995) Ultramicroscopy , vol.58 , pp. 393-402
    • Liu, Y.1    Penczek, P.A.2    McEwen, B.F.3    Frank, J.4
  • 57
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 59
    • 0037403822 scopus 로고    scopus 로고
    • Cryoelectron microscopy of refrozen cryosections
    • Luther PK, Morris EP. 2003. Cryoelectron microscopy of refrozen cryosections. J. Struct. Biol. 142:233-40
    • (2003) J. Struct. Biol. , vol.142 , pp. 233-240
    • Luther, P.K.1    Morris, E.P.2
  • 60
    • 0029885693 scopus 로고    scopus 로고
    • Proposal for a new distributed database of macromolecular and subcellular structures from different areas of microscopy
    • Marabini R, Vaquerizo C, Fernández JJ, Carazo JM, Engel A, Frank J. 1996. Proposal for a new distributed database of macromolecular and subcellular structures from different areas of microscopy. J. Struct. Biol. 116:161-66
    • (1996) J. Struct. Biol. , vol.116 , pp. 161-166
    • Marabini, R.1    Vaquerizo, C.2    Fernández, J.J.3    Carazo, J.M.4    Engel, A.5    Frank, J.6
  • 62
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • Mastronarde DN. 1997. Dual-axis tomography: an approach with alignment methods that preserve resolution. J. Struct. Biol. 120:343-52
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 63
    • 0033573131 scopus 로고    scopus 로고
    • The Escherichia coli large ribosomal subunit at 7.5 Å resolution
    • 61a. Matadeen R, Patwardhan A, Gowen B, Orlova EV, Pape T, et al. 1999. The Escherichia coli large ribosomal subunit at 7.5 Å resolution. Structure 7:1575-83
    • (1999) Structure , vol.7 , pp. 1575-1583
    • Matadeen, R.1    Patwardhan, A.2    Gowen, B.3    Orlova, E.V.4    Pape, T.5
  • 64
    • 0029379689 scopus 로고
    • The relevance of dose-fractionation in tomography of radiation-sensitive specimens
    • McEwen BF, Downing KH, Glaeser RM. 1995. The relevance of dose-fractionation in tomography of radiation-sensitive specimens. Ultramicroscopy 60:357-73
    • (1995) Ultramicroscopy , vol.60 , pp. 357-373
    • McEwen, B.F.1    Downing, K.H.2    Glaeser, R.M.3
  • 65
    • 0036414847 scopus 로고    scopus 로고
    • Use of frozen-hydrated axonemes to assess imaging parameters and resolution limits in cryoelectron tomography
    • McEwen BF, Marko M, Hsieh CE, Mannella C. 2002. Use of frozen-hydrated axonemes to assess imaging parameters and resolution limits in cryoelectron tomography. J. Struct. Biol. 138:47-57
    • (2002) J. Struct. Biol. , vol.138 , pp. 47-57
    • McEwen, B.F.1    Marko, M.2    Hsieh, C.E.3    Mannella, C.4
  • 66
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O, Weber I, Frangakis AS, Nicastro D, Gerisch G, Baumeister W. 2002. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 298:1209-13
    • (2002) Science , vol.298 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 67
    • 18744386656 scopus 로고    scopus 로고
    • Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: A multifunctional catalytic machine
    • Milne JLS, Shi D, Rosenthal PB, Sunshine JS, Domingo GJ, et al. 2002. Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: a multifunctional catalytic machine. EMBO J. 21:5587-98
    • (2002) EMBO J. , vol.21 , pp. 5587-5598
    • Milne, J.L.S.1    Shi, D.2    Rosenthal, P.B.3    Sunshine, J.S.4    Domingo, G.J.5
  • 68
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A, Fujiyoshi Y, Unwin N. 2003. Structure and gating mechanism of the acetylcholine receptor pore. Nature 424:949-55
    • (2003) Nature , vol.424 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 69
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillovirus capsid
    • Modis Y, Trus BL, Harrison SC. 2002. Atomic model of the papillovirus capsid. EMBO J. 21:4754-62
    • (2002) EMBO J. , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 70
    • 0034696756 scopus 로고    scopus 로고
    • The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 Å resolution
    • Mueller F, Sommer I, Baranov P, Matadeen R, Stoldt M, et al. 2000. The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 Å resolution. J. Mol. Biol. 298:35-59
    • (2000) J. Mol. Biol. , vol.298 , pp. 35-59
    • Mueller, F.1    Sommer, I.2    Baranov, P.3    Matadeen, R.4    Stoldt, M.5
  • 73
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ-tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH. 1998. Structure of the αβ-tubulin dimer by electron crystallography. Nature 391:199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 74
    • 0038159661 scopus 로고    scopus 로고
    • Three-dimensional organization of basal bodies from wildtype and δ-tubulin deletion strains of Chlamydomonas reinhardtii
    • O'Toole ET, Giddings TH, McIntosh JR, Dutcher SK. 2003. Three-dimensional organization of basal bodies from wildtype and δ-tubulin deletion strains of Chlamydomonas reinhardtii. Mol. Biol. Cell 14:2999-3012
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2999-3012
    • O'Toole, E.T.1    Giddings, T.H.2    McIntosh, J.R.3    Dutcher, S.K.4
  • 75
    • 0020536972 scopus 로고
    • Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs
    • Oettl H, Hegerl R, Hoppe W. 1983. Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs. J. Mol. Biol. 163:431-50
    • (1983) J. Mol. Biol. , vol.163 , pp. 431-450
    • Oettl, H.1    Hegerl, R.2    Hoppe, W.3
  • 76
    • 0037451286 scopus 로고    scopus 로고
    • Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy
    • Orlova EV, Gowen B, Dröge A, Stiege A, Weise F, et al. 2003. Structure of a viral DNA gatekeeper at 10 Å resolution by cryo-electron microscopy. EMBO J. 22:1255-62
    • (2003) EMBO J. , vol.22 , pp. 1255-1262
    • Orlova, E.V.1    Gowen, B.2    Dröge, A.3    Stiege, A.4    Weise, F.5
  • 78
    • 0035139811 scopus 로고    scopus 로고
    • Subcellular localization of Rab17 by cryoimmunogold electron microscopy in epithelial cells grown on polycarbonate filters
    • Peters PJ, Hunziker W. 2001. Subcellular localization of Rab17 by cryoimmunogold electron microscopy in epithelial cells grown on polycarbonate filters. Methods Enzymol. 329:210-25
    • (2001) Methods Enzymol. , vol.329 , pp. 210-225
    • Peters, P.J.1    Hunziker, W.2
  • 79
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50 S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J. 1987. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50 S ribosomal subunit of Escherichia coli. J. Microsc. 146:113-36
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 80
    • 0015116113 scopus 로고
    • Three-dimensional reconstruction from radiographs and electron micrographs: Application of convolutions instead of Fourier transforms
    • Ramachandran GN, Lakshminarayanan AV. 1971. Three-dimensional reconstruction from radiographs and electron micrographs: application of convolutions instead of Fourier transforms. Proc. Natl. Acad. Sci. USA 68:2236-40
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2236-2240
    • Ramachandran, G.N.1    Lakshminarayanan, A.V.2
  • 81
    • 0031413603 scopus 로고    scopus 로고
    • Low-dose automated electron tomography: A recent implementation
    • Rath BK, Marko M, Radermacher M, Frank J. 1997. Low-dose automated electron tomography: a recent implementation. J. Struct. Biol. 120:210-18
    • (1997) J. Struct. Biol. , vol.120 , pp. 210-218
    • Rath, B.K.1    Marko, M.2    Radermacher, M.3    Frank, J.4
  • 82
    • 0033776245 scopus 로고    scopus 로고
    • Docking structures of domains into maps from cryo-electron microscopy using local correlation
    • Roseman AM. 2000. Docking structures of domains into maps from cryo-electron microscopy using local correlation. Acta Crystallogr. D 56:1332-40
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1332-1340
    • Roseman, A.M.1
  • 83
    • 0035783056 scopus 로고    scopus 로고
    • Combining electron microscopic with X-ray crystallographic structures
    • Rossmann MG, Bernal R, Pletnev SV. 2001. Combining electron microscopic with X-ray crystallographic structures. J. Struct. Biol. 136:190-200
    • (2001) J. Struct. Biol. , vol.136 , pp. 190-200
    • Rossmann, M.G.1    Bernal, R.2    Pletnev, S.V.3
  • 84
    • 0033776856 scopus 로고    scopus 로고
    • Macromolecular structure determination by cryo-electron microscopy
    • Saibil HR. 2000. Macromolecular structure determination by cryo-electron microscopy. Acta Crystallogr. D 56:1215-22
    • (2000) Acta Crystallogr. D , vol.56 , pp. 1215-1222
    • Saibil, H.R.1
  • 86
    • 0031767521 scopus 로고    scopus 로고
    • Electron beam-induced changes in vitreous sections of biological samples
    • Sartori Blanc N, Studer D, Ruhl K, Dubochet J. 1998. Electron beam-induced changes in vitreous sections of biological samples. J. Microsc. 192:194-201
    • (1998) J. Microsc. , vol.192 , pp. 194-201
    • Sartori Blanc, N.1    Studer, D.2    Ruhl, K.3    Dubochet, J.4
  • 87
    • 0021119424 scopus 로고
    • Three-dimensional reconstruction of imperfect two-dimensional crystals
    • Saxton WO, Baumeister W, Hahn M. 1984. Three-dimensional reconstruction of imperfect two-dimensional crystals. Ultramicroscopy 13:57-70
    • (1984) Ultramicroscopy , vol.13 , pp. 57-70
    • Saxton, W.O.1    Baumeister, W.2    Hahn, M.3
  • 88
    • 0037333340 scopus 로고    scopus 로고
    • The next ice age: Cryo-electron tomography of intact cells
    • Steven AC, Aebi U. 2003. The next ice age: cryo-electron tomography of intact cells. Trends Cell Biol. 13:107-10
    • (2003) Trends Cell Biol. , vol.13 , pp. 107-110
    • Steven, A.C.1    Aebi, U.2
  • 89
    • 0037453221 scopus 로고    scopus 로고
    • Cryo-electron tomography provides novel insights into nuclear pore architecture: Implications for nucleocytoplasmic transport
    • Stoffler D, Feja B, Fahrenkrog B, Walz J, Typke D, Aebi U. 2003. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328:119-30
    • (2003) J. Mol. Biol. , vol.328 , pp. 119-130
    • Stoffler, D.1    Feja, B.2    Fahrenkrog, B.3    Walz, J.4    Typke, D.5    Aebi, U.6
  • 90
    • 0033956806 scopus 로고    scopus 로고
    • Minimal compression of ultrathin sections with use of an oscillating diamond knife
    • Studer D, Gnaegi H. 2000. Minimal compression of ultrathin sections with use of an oscillating diamond knife. J. Microsc. 197:94-100
    • (2000) J. Microsc. , vol.197 , pp. 94-100
    • Studer, D.1    Gnaegi, H.2
  • 91
    • 0035462162 scopus 로고    scopus 로고
    • A new approach for cryofixation by high-pressure freezing
    • Studer D, Graber W, Al-Amoudi A, Eggli P. 2001. A new approach for cryofixation by high-pressure freezing. J. Microsc. 203:285-94
    • (2001) J. Microsc. , vol.203 , pp. 285-294
    • Studer, D.1    Graber, W.2    Al-Amoudi, A.3    Eggli, P.4
  • 92
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S, Henderson R. 2000. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406:653-57
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 94
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor KA, Glaeser RM. 1974. Electron diffraction of frozen, hydrated protein crystals. Science 186:1036-37
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 96
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin PNT, Henderson R. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:425-40
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 97
    • 0242407184 scopus 로고    scopus 로고
    • Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
    • 94a. Valle M, Zavialov A, Li W, Stagg SM, Sengupta J, et al. 2003. Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Nat. Struct. Biol. 10:899-906
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 899-906
    • Valle, M.1    Zavialov, A.2    Li, W.3    Stagg, S.M.4    Sengupta, J.5
  • 99
    • 0023102907 scopus 로고
    • Angular reconstitution: A posteriori assignment of projection directions for 3D reconstructions
    • Van Heel M. 1987. Angular reconstitution: a posteriori assignment of projection directions for 3D reconstructions. Ultramicroscopy 21:111-24
    • (1987) Ultramicroscopy , vol.21 , pp. 111-124
    • Van Heel, M.1
  • 100
  • 102
    • 0031423486 scopus 로고    scopus 로고
    • Electron tomography of single ice-embedded macromolecules: Three-dimensional alignment and classification
    • Walz J, Typke D, Nitsch M, Koster AJ, Hegerl R, Baumeister W. 1997. Electron tomography of single ice-embedded macromolecules: three-dimensional alignment and classification. J. Struct. Biol. 120:387-95
    • (1997) J. Struct. Biol. , vol.120 , pp. 387-395
    • Walz, J.1    Typke, D.2    Nitsch, M.3    Koster, A.J.4    Hegerl, R.5    Baumeister, W.6
  • 103
    • 0042167432 scopus 로고    scopus 로고
    • Focus gradient correction applied to tilt series image data used in electron tomography
    • Winkler H, Taylor KA. 2003. Focus gradient correction applied to tilt series image data used in electron tomography. J. Struct. Biol. 143:24-32
    • (2003) J. Struct. Biol. , vol.143 , pp. 24-32
    • Winkler, H.1    Taylor, K.A.2
  • 104
    • 0037285752 scopus 로고    scopus 로고
    • A core-weighted fitting method for docking atomic structures into low-resolution maps: Application to cryoelectron microscopy
    • Wu X, Milne JLS, Borgnia MJ, Rostapshov AV, Subramaniam S, Brooks BR. 2003. A core-weighted fitting method for docking atomic structures into low-resolution maps: application to cryoelectron microscopy. J. Struct. Biol. 141:63-76
    • (2003) J. Struct. Biol. , vol.141 , pp. 63-76
    • Wu, X.1    Milne, J.L.S.2    Borgnia, M.J.3    Rostapshov, A.V.4    Subramaniam, S.5    Brooks, B.R.6
  • 105
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K, Maki-Yonekura S, Namba K. 2003. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424:643-50
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 106
    • 0035783259 scopus 로고    scopus 로고
    • Automated data collection with a Tecnai 12 electron microscope: Applications for molecular imaging by cryomicroscopy
    • Zhang P, Beatty A, Milne JLS, Subramaniam S. 2001. Automated data collection with a Tecnai 12 electron microscope: applications for molecular imaging by cryomicroscopy. J. Struct. Biol. 135:251-61
    • (2001) J. Struct. Biol. , vol.135 , pp. 251-261
    • Zhang, P.1    Beatty, A.2    Milne, J.L.S.3    Subramaniam, S.4
  • 107
    • 10744220292 scopus 로고    scopus 로고
    • Automated image acquisition and processing using a new generation of 4K x 4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies
    • Zhang P, Borgnia MJ, Mooney P, Shi D, Pan M, et al. 2003. Automated image acquisition and processing using a new generation of 4K x 4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies. J. Struct. Biol. 143:135-44
    • (2003) J. Struct. Biol. , vol.143 , pp. 135-144
    • Zhang, P.1    Borgnia, M.J.2    Mooney, P.3    Shi, D.4    Pan, M.5
  • 108
    • 0034814786 scopus 로고    scopus 로고
    • Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus
    • Zhou ZH, Baker ML, Jiang W, Dougherty M, Jakana J, et al. 2001. Electron cryomicroscopy and bioinformatics suggest protein fold models for rice dwarf virus. Nat. Struct. Biol. 8:868-73
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 868-873
    • Zh, Z.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Jakana, J.5
  • 110
    • 0043160452 scopus 로고    scopus 로고
    • Correction of autofocusing errors due to specimen tilt for automated electron tomography
    • Ziese U, Geerts WJC, Van Der Krift TP, Verkleij AJ, Koster AJ. 2003. Correction of autofocusing errors due to specimen tilt for automated electron tomography. J. Microsc. 211:179-85
    • (2003) J. Microsc. , vol.211 , pp. 179-185
    • Ziese, U.1    Geerts, W.J.C.2    Van Der Krift, T.P.3    Verkleij, A.J.4    Koster, A.J.5
  • 111
    • 0036125507 scopus 로고    scopus 로고
    • Automated high-throughput electron tomography by pre-calibration of image shifts
    • Ziese U, Janssen AH, Murk J-L, Geerts WJC, Van der Krift T, et al. 2002. Automated high-throughput electron tomography by pre-calibration of image shifts. J. Microsc. 205:187-200
    • (2002) J. Microsc. , vol.205 , pp. 187-200
    • Ziese, U.1    Janssen, A.H.2    Murk, J.-L.3    Geerts, W.J.C.4    Van Der Krift, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.