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Volumn 6, Issue 5, 1996, Pages 585-594

Low resolution meets high: Towards a resolution continuum from cells to atoms

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC PARTICLE; DATA ANALYSIS; MACROMOLECULE; OPTICAL RESOLUTION; PRIORITY JOURNAL; REVIEW; TRANSMISSION ELECTRON MICROSCOPY; X RAY CRYSTALLOGRAPHY;

EID: 0030272365     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(96)80023-6     Document Type: Article
Times cited : (75)

References (95)
  • 1
    • 0000490047 scopus 로고
    • The viral canyon
    • Hogle JM: The viral canyon. Curr Biol 1993, 3:278-281.
    • (1993) Curr Biol , vol.3 , pp. 278-281
    • Hogle, J.M.1
  • 2
    • 0028221575 scopus 로고
    • Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography
    • Chiu W, Smith TJ: Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography. Curr Biol 1994, 4:219-224.
    • (1994) Curr Biol , vol.4 , pp. 219-224
    • Chiu, W.1    Smith, T.J.2
  • 4
    • 0028831519 scopus 로고
    • Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus
    • Smith TJ, Mosser AG, Baker TS: Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus. Semin Virol 1995, 6:233-242.
    • (1995) Semin Virol , vol.6 , pp. 233-242
    • Smith, T.J.1    Mosser, A.G.2    Baker, T.S.3
  • 5
    • 0030026807 scopus 로고    scopus 로고
    • Functional implications of protein-protein interactions in icosahedral viruses
    • Johnson JE: Functional implications of protein-protein interactions in icosahedral viruses. Proc Natl Acad Sei USA 1996, 93:27-33.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 27-33
    • Johnson, J.E.1
  • 6
    • 0027917984 scopus 로고
    • Myosin-actin motors: The partnership goes atomic
    • Reedy MK: Myosin-actin motors: the partnership goes atomic. Structure 1993, 1:1-5.
    • (1993) Structure , vol.1 , pp. 1-5
    • Reedy, M.K.1
  • 7
    • 0028256424 scopus 로고
    • The three-dimensional structure of a molecular motor
    • Rayment l, Holden HM: The three-dimensional structure of a molecular motor. Trends Biochem Sei 1994, 19:129-134.
    • (1994) Trends Biochem Sei , vol.19 , pp. 129-134
    • Rayment, L.1    Holden, H.M.2
  • 8
    • 0028988935 scopus 로고
    • New insights into actin filament dynamics
    • Egelman EH, Orlova A: New insights into actin filament dynamics. Curr Opin Struct Biol 1995, 52:172-180.
    • (1995) Curr Opin Struct Biol , vol.52 , pp. 172-180
    • Egelman, E.H.1    Orlova, A.2
  • 9
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan RA: Protein-protein interactions in the rigor actomyosin complex. Proc Natl Acad Sei USA 1996, 93:21-26.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 10
    • 0027264030 scopus 로고
    • What does electron cryomicroscopy provide that X-ray crystallography and NMR spectroscopy cannot?
    • Chiu W: What does electron cryomicroscopy provide that X-ray crystallography and NMR spectroscopy cannot? Annu Rev Biophys Biomol Struct 1993, 22:233-255.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 233-255
    • Chiu, W.1
  • 11
    • 0028773901 scopus 로고
    • Solving the structures of macromolecular complexes
    • Holmes KC: Solving the structures of macromolecular complexes. Structure 1994, 2:589-593.
    • (1994) Structure , vol.2 , pp. 589-593
    • Holmes, K.C.1
  • 12
    • 0027909845 scopus 로고
    • Architecture of the invisible
    • Thomas JM: Architecture of the invisible. Nature 1994, 364:478-482.
    • (1994) Nature , vol.364 , pp. 478-482
    • Thomas, J.M.1
  • 13
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R, Unwin PNT: Three-dimensional model of purple membrane obtained by electron microscopy. Nature 1975, 257:28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 14
    • 0017853336 scopus 로고
    • Structure determination of frozen, hydrated, crystalline biological specimens
    • Taylor KA: Structure determination of frozen, hydrated, crystalline biological specimens. J Microsc 1978, 112:115-125.
    • (1978) J Microsc , vol.112 , pp. 115-125
    • Taylor, K.A.1
  • 15
    • 0021153153 scopus 로고
    • Molecular structure determination of crystalline specimens in frozen aqueous solutions
    • Milligan RA, Brisson A, Unwin PNT: Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicroscopy 1984, 13:1-10.
    • (1984) Ultramicroscopy , vol.13 , pp. 1-10
    • Milligan, R.A.1    Brisson, A.2    Unwin, P.N.T.3
  • 16
    • 0023053060 scopus 로고
    • Electron microscopy of frozen-hydrated biological material
    • Stewart M, Vigers G: Electron microscopy of frozen-hydrated biological material. Nature 1986, 319:631-636.
    • (1986) Nature , vol.319 , pp. 631-636
    • Stewart, M.1    Vigers, G.2
  • 18
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH: Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 1990, 213:899-929.
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 19
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W, Wang DN, Fujiyoshi Y: Atomic model of plant light-harvesting complex by electron crystallography. Nature 1994, 367:614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 20
    • 0024961660 scopus 로고
    • Visualization of αhelices in tobacco mosaic virus by cryo-electron microscopy
    • Jeng TW, Crowther RA, Stubbs G, Chui W: Visualization of αhelices in tobacco mosaic virus by cryo-electron microscopy. J Mol Biol 1989, 205:251-257.
    • (1989) J Mol Biol , vol.205 , pp. 251-257
    • Jeng, T.W.1    Crowther, R.A.2    Stubbs, G.3    Chui, W.4
  • 21
    • 0029042213 scopus 로고
    • Structure of bacterial flagellar filaments at 11 Å resolution: Packing of the α-helices
    • Morgan DG, Owen C, Melanson LAV DeRosier DJ: Structure of bacterial flagellar filaments at 11 Å resolution: packing of the α-helices. J Mol Biol 1995, 249:88-110.
    • (1995) J Mol Biol , vol.249 , pp. 88-110
    • Morgan, D.G.1    Owen, C.2    Melanson, L.A.V.3    DeRosier, D.J.4
  • 22
    • 0029039662 scopus 로고
    • The structure.of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy
    • Mimori Y, Yamashita I, Murata K, Fujiyoshi Y, Yonekura K, Toyoshima C, Namba K: The structure.of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy. J Mol Biol 1995, 249:69-87.
    • (1995) J Mol Biol , vol.249 , pp. 69-87
    • Mimori, Y.1    Yamashita, I.2    Murata, K.3    Fujiyoshi, Y.4    Yonekura, K.5    Toyoshima, C.6    Namba, K.7
  • 23
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N: Acetylcholine receptor channel imaged in the open state. Nature 1995, 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 24
    • 0028773272 scopus 로고
    • Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and x-ray crystallography
    • Cheng RH, Reddy V, Olson NH, Fisher A, Baker TS, Johnson JE: Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and x-ray crystallography. Structure 1994, 2:271-282.
    • (1994) Structure , vol.2 , pp. 271-282
    • Cheng, R.H.1    Reddy, V.2    Olson, N.H.3    Fisher, A.4    Baker, T.S.5    Johnson, J.E.6
  • 25
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy
    • Stewart PL, Fuller SD, Burnett RM: Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J 1993, 12:2589-2599.
    • (1993) EMBO J , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 26
    • 0027121512 scopus 로고
    • ab interaction site (footprint) on an icosahedral virus by cryo-electron microscopy and x-ray crystallography
    • ab interaction site (footprint) on an icosahedral virus by cryo-electron microscopy and x-ray crystallography. Nature 1992, 355:275-278.
    • (1992) Nature , vol.355 , pp. 275-278
    • Wang, G.1    Porta, C.2    Chen, Z.3    Baker, T.S.4    Johnson, J.E.5
  • 28
    • 0028245914 scopus 로고
    • Three-dimensional structure of membranebound annexin V: A correlative electron microscopy-X-ray crystallographic study
    • Voges D, Berendes R, Burger A, Démange P, Baumeister W, Huber R: Three-dimensional structure of membranebound annexin V: a correlative electron microscopy-X-ray crystallographic study. J Mol Biol 1994, 238:199-213.
    • (1994) J Mol Biol , vol.238 , pp. 199-213
    • Voges, D.1    Berendes, R.2    Burger, A.3    Démange, P.4    Baumeister, W.5    Huber, R.6
  • 29
    • 0029644486 scopus 로고
    • DMA packaging intermediates of bacteriophage φX174
    • Hag LL, Olson NH, Dokland T, Music CL, Cheng RH, Bowen Z, McKenna R, Rossmann MG, Baker TS, Incardona NL: DMA packaging intermediates of bacteriophage φX174. Structure 1995, 3:353-363. Modeling of the atomic structures of the F and G virion proteins (from the crystal structure of the 70S virion) into cryoEM reconstructions of 108S procapsids and 132S provirions shows that the G and F proteins undergo minor and major conformational changes, respectively; these changes are believed to help facilitate viral assembly.
    • (1995) Structure , vol.3 , pp. 353-363
    • Hag, L.L.1    Olson, N.H.2    Dokland, T.3    Music, C.L.4    Cheng, R.H.5    Bowen, Z.6    McKenna, R.7    Rossmann, M.G.8    Baker, T.S.9    Incardona, N.L.10
  • 30
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by x-ray crystallography and cryo-electron microscopy
    • Speir JA, Munshi S, Wang G, Baker TS, Johnson JE: Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by x-ray crystallography and cryo-electron microscopy. Structure 1995, 3:63-78. The 3.2 Å structure of the native virus is determined by X-ray crystallography. The atomic-resolution subunit model is then fitted to the cryoEM density for a swollen form of the virus, demonstrating that electrostatic repulsion from ionized acidic residues causes the swelling at neutral pH in the absence of divalent metal ions.
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 31
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker TS, Cheng RH: A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J Struct Biol 1996, 116:120-130.
    • (1996) J Struct Biol , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 32
    • 0029670614 scopus 로고    scopus 로고
    • Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monoloayers by electron crystallography
    • Avila-Saker AJ, Chiu W: Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monoloayers by electron crystallography. Biophys J1996, 70:57-68. Two dimensional crystals of streptavidin are ordered to 2.5 Å resolution. Electron-diffraction data are collected and used for the refinement of the available X-ray atomic model using the program X-PLOR. An agreement factor of 18% is obtained while maintaining good geometry in the protein. The coordinates of the model refined against the electron diffraction data are closely similar to the X-ray coordinates.
    • (1996) Biophys J , vol.70 , pp. 57-68
    • Avila-Saker, A.J.1    Chiu, W.2
  • 33
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for virus neutralization and antibody flexibility
    • Smith TJ, Olson NH, Cheng RH, Chase ES, Baker TS: Structure of a human rhinovirus-bivalently bound antibody complex: implications for virus neutralization and antibody flexibility. Proc Natl Acad Sei USA 1993, 90:7015-7018.
    • (1993) Proc Natl Acad Sei USA , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 34
    • 0029562245 scopus 로고
    • A 35-Å tail swing in brush border myosin i on AOP release
    • ̇̇]. Docking of the homologous region of the X-ray structure of skeletal S1 (the motor domain) into the EM maps demonstrates that even a limited amount of highresolution information can provide insight into the nature of the changes: the light-chain region rotates as a rigid body about its junction with the immobile motor domain.
    • (1995) Nature , vol.378 , pp. 751-753
    • Jontes, J.D.1    Wilson-Kubalek, E.M.2    Milligan, R.A.3
  • 39
    • 0028919758 scopus 로고
    • Three-dimensional structure of an enveloped alphavirus with T=4 icosahedral symmetry
    • Cheng RH, Kuhn RJ, Olson NH, Rossmann MG, Choi HK, Smith TJ, Baker TS: Three-dimensional structure of an enveloped alphavirus with T=4 icosahedral symmetry. Cell 1995, 80:621-630. Modeling of atomic structure of the Sindbis core protein into the cryoEM reconstruction of the nucleocapsid portion of Ross River virus shows that the nucleocapsid protein does not associate as dimers, as predicted on the basis of crystallographic experiments. Instead, the capsid proteins are arranged as pentamers and hexamers in a T=4 lattice and in one-to-one association with the 240 E1·E2 glycoprotein heterodimers.
    • (1995) Cell , vol.80 , pp. 621-630
    • Cheng, R.H.1    Kuhn, R.J.2    Olson, N.H.3    Rossmann, M.G.4    Choi, H.K.5    Smith, T.J.6    Baker, T.S.7
  • 41
    • 0028032395 scopus 로고
    • Viral cell recognition and entry
    • Rossmann MG: Viral cell recognition and entry. Protein Sei 1994, 3:1712-1725.
    • (1994) Protein Sei , vol.3 , pp. 1712-1725
    • Rossmann, M.G.1
  • 44
    • 0029645318 scopus 로고
    • The 70S Escherichia coli ribosome at 23 Åresolution: Fitting the ribosomal RNA
    • Stark H, Mueller F, Orlova EV, Schatz M, Dubel P, Erdemir T, Zemlin F, Brimacombe R, Van Heel M: The 70S Escherichia coli ribosome at 23 Åresolution: fitting the ribosomal RNA. Structure 1995, 3:815-821. The authors describe the preliminary fitting of the double helical regions of a rRNA, from a 3D model based on biochemical data, to a cryoEM reconstruction of the 70S ribosome. The reconstruction shows an extensive system of channels within the 50S subunil and a gap between the 30S and 50S subunits, reported to be ideally shaped to accommodate two tRNA molecules.
    • (1995) Structure , vol.3 , pp. 815-821
    • Stark, H.1    Mueller, F.2    Orlova, E.V.3    Schatz, M.4    Dubel, P.5    Erdemir, T.6    Zemlin, F.7    Brimacombe, R.8    Van Heel, M.9
  • 47
    • 0027099852 scopus 로고
    • Chase ES: Purification and crystallization of intact human rhivovirus complexed with a neutralizing Fab
    • Smith TJ. Chase ES: Purification and crystallization of intact human rhivovirus complexed with a neutralizing Fab. Virology 1993. 191:600-606.
    • (1993) Virology , vol.191 , pp. 600-606
    • Smith, T.J.1
  • 48
    • 0020031457 scopus 로고
    • Polyoma virus capsid crystal structure at 22.5 Å resolution
    • Payment I, Baker TS, Caspar OLD, Murakami WR: Polyoma virus capsid crystal structure at 22.5 Å resolution. Nature 1982, 295:110-115.
    • (1982) Nature , vol.295 , pp. 110-115
    • Payment, I.1    Baker, T.S.2    Caspar, O.L.D.3    Murakami, W.R.4
  • 49
    • 84977300366 scopus 로고
    • A description of the techniques and application of molecular replacement used to determine the structure of polyoma virus capsids at 22.5 Å resolution
    • Rayment I, Baker TS, Caspar OLD: A description of the techniques and application of molecular replacement used to determine the structure of polyoma virus capsids at 22.5 Å resolution. Acta Crystallogr IB] 1983, 39:505-516.
    • (1983) Acta Crystallogr IB , vol.39 , pp. 505-516
    • Rayment, I.1    Baker, T.S.2    Caspar, O.L.D.3
  • 50
    • 0028726095 scopus 로고
    • How chaperones tell wrong from right
    • Saibil HR: How chaperones tell wrong from right. Nat Struct Biol 1994, 1:838-842.
    • (1994) Nat Struct Biol , vol.1 , pp. 838-842
    • Saibil, H.R.1
  • 51
    • 0028889613 scopus 로고
    • Human erythrocyte catalase: 2-D crystal nucleation and production of multiple crystal forms
    • Harris JR, Holzenburg A: Human erythrocyte catalase: 2-D crystal nucleation and production of multiple crystal forms. J Struct e/b/1995, 115:102-112.
    • (1995) J Struct E/b , vol.115 , pp. 102-112
    • Harris, J.R.1    Holzenburg, A.2
  • 52
    • 0028618538 scopus 로고
    • Supramolecular self-assembly of glutamine synthetase: Mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking
    • Dabrowski JJ, Yanchunas J Jr, Villafranca BC, Dietze EC, Schurke P, Atkins WM: Supramolecular self-assembly of glutamine synthetase: mutagenesis of a novel intermolecular metal binding site required for dodecamer stacking. Biochemistry 1994. 33:14957-14964.
    • (1994) Biochemistry , vol.33 , pp. 14957-14964
    • Dabrowski, J.J.1    Yanchunas Jr., J.2    Villafranca, B.C.3    Dietze, E.C.4    Schurke, P.5    Atkins, W.M.6
  • 53
    • 0028294213 scopus 로고
    • Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films
    • Celia H, Hoermann L, Schultz P, Lebeau L, Mallouh V, Wigle DB, Wang JC, Mioskowski C, Oudet P: Three-dimensional model of Escherichia coli gyrase B subunit crystallized in two-dimensions on novobiocin-linked phospholipid films. J Mol Biol 1994, 236:618-628.
    • (1994) J Mol Biol , vol.236 , pp. 618-628
    • Celia, H.1    Hoermann, L.2    Schultz, P.3    Lebeau, L.4    Mallouh, V.5    Wigle, D.B.6    Wang, J.C.7    Mioskowski, C.8    Oudet, P.9
  • 54
    • 0028590161 scopus 로고
    • Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid
    • Kubalek EW, LeGrice SFJ, Brown PO: Two-dimensional crystallization of histidine-tagged, HIV-1 reverse transcriptase promoted by a novel nickel-chelating lipid. J Struct Biol 1994, 113:117-123.
    • (1994) J Struct Biol , vol.113 , pp. 117-123
    • Kubalek, E.W.1    LeGrice, S.F.J.2    Brown, P.O.3
  • 55
    • 0028181107 scopus 로고
    • Microcrystals of the beta 1 isoenzyme of protein kinase C: An electron microscopic study
    • Newman RH, Carpenter E, Freemont PS, Blundell TL, Parker PJ: Microcrystals of the beta 1 isoenzyme of protein kinase C: an electron microscopic study. Biochem J 1994, 298:391-393.
    • (1994) Biochem J , vol.298 , pp. 391-393
    • Newman, R.H.1    Carpenter, E.2    Freemont, P.S.3    Blundell, T.L.4    Parker, P.J.5
  • 58
    • 0028266195 scopus 로고
    • Reed RA, McDermott MR, Shipley GG: Orientation of cholera toxin bound to model membranes
    • Cabral-Lilly D, Sosinsky GE. Reed RA, McDermott MR, Shipley GG: Orientation of cholera toxin bound to model membranes. Biophys J 1994, 66:935-941.
    • (1994) Biophys J , vol.66 , pp. 935-941
    • Cabral-Lilly, D.1    Sosinsky, G.E.2
  • 60
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC: Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994, 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 61
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton SA, Calder U, Ruigrok RW, Skehel JJ, Steinhauer DA, Wiley DC: Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO J 1995, 14:240-246.
    • (1995) EMBO J , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, U.2    Ruigrok, R.W.3    Skehel, J.J.4    Steinhauer, D.A.5    Wiley, D.C.6
  • 62
    • 0030584656 scopus 로고    scopus 로고
    • Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila
    • Savage H, Cyrklaff M, Montoya G, Kühlbrandt W, Sinning I: Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila. Structure 1996, 4:243-252. The two dimensional structure of LH(II) from Rhodovulum sulfidophilum is determined at 7 Å resolution by cryoEM. The structure is compared with the 2.5 Åresolution atomic model of LH(II) from Rhodopseudomonas acidophila. The two structures correlate very well with the major difference being a slight displacement of the outer helices, perhaps attributable to a different degree of tilt in these helices in the two structures.
    • (1996) Structure , vol.4 , pp. 243-252
    • Savage, H.1    Cyrklaff, M.2    Montoya, G.3    Kühlbrandt, W.4    Sinning, I.5
  • 63
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert FA, Henn C, Engel A: Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science 1995. 268:92-94. Atomic models of protein-protein and lipid-protein interactions are developed on the basis of the X-ray crystal structure of the OmpF porin trimer and topographs recorded by atomic force microscopy (AFM) of 2D crystals reconstituted in the presence of lipids. The bilayer is modeled with kinked lipids by fitting the head groups to contours determined with AFM. The potential of AFM to monitor conformational changes at high resolution is clearly demonstrated.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 66
    • 0028579523 scopus 로고
    • A structure for the signal sequence binding protein SRP54: 3D reconstruction from STEM images of single molecules
    • Czarnota GJ, Andrews DW, Farrow NA, Ottensmeyer FP: A structure for the signal sequence binding protein SRP54: 3D reconstruction from STEM images of single molecules. J Struct Biol 1994, 113:35-46.
    • (1994) J Struct Biol , vol.113 , pp. 35-46
    • Czarnota, G.J.1    Andrews, D.W.2    Farrow, N.A.3    Ottensmeyer, F.P.4
  • 67
    • 0028969420 scopus 로고
    • Chiu W: Three-dimensional structure of the acrosomal filament of Limulus sperm by 400 kV electron cryomicroscopy
    • Schmidt MF, Jakana J, Matsudaira P. Chiu W: Three-dimensional structure of the acrosomal filament of Limulus sperm by 400 kV electron cryomicroscopy. Biophys J 1995, 68:85-11S. The chemical basis for straightening the acrosomal process in the fertilization reaction of Limulus sperm is examined. An acrosomal bundle formed of an actin filament with associated scruin molecules is imaged at 7Å resolution using cryoEM and image processing. Fitting the atomic model of F-actin to the EM map allows the identification of residues on actin that interact with scruin.
    • (1995) Biophys J , vol.68
    • Schmidt, M.F.1    Jakana, J.2    Matsudaira, P.3
  • 68
    • 0028115630 scopus 로고
    • Threedimensional structure of a single filament in the Limulus acrosomal bundle: Scruin binds to homologous helix-loop-beta motifs in actin
    • Schmid MF, Agris JM, Jakana J, Matsudaira P, Chiu W: Threedimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin. J Cell Biol 1994, 124:341-350.
    • (1994) J Cell Biol , vol.124 , pp. 341-350
    • Schmid, M.F.1    Agris, J.M.2    Jakana, J.3    Matsudaira, P.4    Chiu, W.5
  • 69
    • 0028971512 scopus 로고
    • A 7-Å projection map of frozen, hydrated acrosomal bundle from Limulus sperm
    • Schmid MF, Jakana J, Chiu W: A 7-Å projection map of frozen, hydrated acrosomal bundle from Limulus sperm. J Struct Biol 1995. 115:209-213.
    • (1995) J Struct Biol , vol.115 , pp. 209-213
    • Schmid, M.F.1    Jakana, J.2    Chiu, W.3
  • 70
    • 0028074267 scopus 로고
    • Combining electron microscopy and X-ray crystallography data to study the structure of F-actin and its implications for thin-filament regulation in muscle
    • Mendelson R, Morris E: Combining electron microscopy and X-ray crystallography data to study the structure of F-actin and its implications for thin-filament regulation in muscle. Adv Exp Med Biol 1994, 358:13-23.
    • (1994) Adv Exp Med Biol , vol.358 , pp. 13-23
    • Mendelson, R.1    Morris, E.2
  • 71
    • 0028298374 scopus 로고
    • The structure of F-actin. Results of global searches using data from electron microscopy and X-ray crystallography
    • Mendelson R, Morris E: The structure of F-actin. Results of global searches using data from electron microscopy and X-ray crystallography. J Mol Biol 1994, 240:138-154.
    • (1994) J Mol Biol , vol.240 , pp. 138-154
    • Mendelson, R.1    Morris, E.2
  • 72
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin: I. Changes in the C terminus
    • Orlova A, Egelman EH: Structural dynamics of F-actin: I. Changes in the C terminus. J Mol Biol 1995, 245:582-597.
    • (1995) J Mol Biol , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 73
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. Cooperativity in structural transitions
    • Orlova A, Prochniewicz E, Egelman EH: Structural dynamics of F-actin: II. Cooperativity in structural transitions, J Mol Biol 1995, 245:598-607.
    • (1995) J Mol Biol , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 74
    • 0028176006 scopus 로고
    • DeRosier D: Determination of the a-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough A, Way M. DeRosier D: Determination of the a-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J Cell Biol 1994, 126:433-443.
    • (1994) J Cell Biol , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2
  • 75
    • 0028863184 scopus 로고
    • Molecular model of an actin filament capped by a severing protein
    • McGough A, Way M: Molecular model of an actin filament capped by a severing protein. J Struct Biol 1995, 115:144-150.
    • (1995) J Struct Biol , vol.115 , pp. 144-150
    • McGough, A.1    Way, M.2
  • 76
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman W, Vibert P, Uman P, Craig R: Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J Mol Biol 1995, 251:191-196. An atomic resolution model of F-actin is fitted to the negative-stain, EM-derived, density of skeletal muscle filaments. A cleft in the F-actin model agrees well with a complimentary feature in the EM map, supporting the fit. The fit of the high-resolution model supports the mechanism by which strong cross-bridge association between actin and myosin is inhibited in relaxed muscle by a troponin-stabilized form of tropomyosin.
    • (1995) J Mol Biol , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 78
    • 0029594551 scopus 로고
    • Three-dimensional reconstruction of thick filaments from rapidly frozen, freeze-substituted tarantula muscle
    • Padron R, Alamo L, Guerrero JR, Granados M: Three-dimensional reconstruction of thick filaments from rapidly frozen, freeze-substituted tarantula muscle. J Struct Biol 1995, 115:250-257.
    • (1995) J Struct Biol , vol.115 , pp. 250-257
    • Padron, R.1    Alamo, L.2    Guerrero, J.R.3    Granados, M.4
  • 79
    • 0028954281 scopus 로고
    • The actomyosin interaction and its control by tropomyosin
    • Holmes KC: The actomyosin interaction and its control by tropomyosin. Biophys J 1995, 68:2S-7S.
    • (1995) Biophys J , vol.68
    • Holmes, K.C.1
  • 80
    • 0028294457 scopus 로고
    • Coiled-coil packing in spermine-induced tropomyosin crystals: A comparative study of three forms
    • Xie X, Rao S, Walian P, Hatch V, Phillips GN Jr, Cohen C: Coiled-coil packing in spermine-induced tropomyosin crystals: a comparative study of three forms. J Mol Biol 1994, 236:1212-1226.
    • (1994) J Mol Biol , vol.236 , pp. 1212-1226
    • Xie, X.1    Rao, S.2    Walian, P.3    Hatch, V.4    Phillips Jr., G.N.5    Cohen, C.6
  • 81
    • 0028237034 scopus 로고
    • The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum. A tentative mechanism for cooperative behavior
    • DeHaas F, VanBruggen EF: The interhexameric contacts in the four-hexameric hemocyanin from the tarantula Eurypelma californicum. A tentative mechanism for cooperative behavior. J Mol Biol 1994, 237:464-478.
    • (1994) J Mol Biol , vol.237 , pp. 464-478
    • DeHaas, F.1    VanBruggen, E.F.2
  • 82
    • 0000284121 scopus 로고
    • Quaternary structure of multihexameric arthropod hemocyanins
    • VanHeel M, Dube P: Quaternary structure of multihexameric arthropod hemocyanins. Micron 1994, 25:387-418.
    • (1994) Micron , vol.25 , pp. 387-418
    • VanHeel, M.1    Dube, P.2
  • 84
    • 0028832525 scopus 로고
    • Three-dimensional reconstruction of Androctonus australis hemocyanin labeled with a monoclonal fab fragment
    • Boisset N, Penczek P, Taveau JC, Lamy J, Frank J, Lamy J: Three-dimensional reconstruction of Androctonus australis hemocyanin labeled with a monoclonal fab fragment J Struct Biol 1995, 115:16-29. The 3D fitting of closely related X-ray structures of Panulirus interruptus hemocyanin and of Fab R19.9 to the cryoEM reconstruction of the scorpion 4 × 6meric hemocyanin-Fab L104 complex localized the epitope to the surface of the Aa6 hemocyanin subunit.
    • (1995) J Struct Biol , vol.115 , pp. 16-29
    • Boisset, N.1    Penczek, P.2    Taveau, J.C.3    Lamy, J.4    Frank, J.5    Lamy, J.6
  • 85
    • 0029645411 scopus 로고
    • Ribosomes seen through a glass less darkly
    • Moore PB: Ribosomes seen through a glass less darkly. Structure 1995, 3:851-852.
    • (1995) Structure , vol.3 , pp. 851-852
    • Moore, P.B.1
  • 86
    • 0028804905 scopus 로고
    • Putative receptor binding sites on enveloped viruses as visualized by cryo-electron microscopy
    • Smith TJ, Cheng RH, Olson NH, Peterson P, Chase E, Kuhn RJ, Baker TS: Putative receptor binding sites on enveloped viruses as visualized by cryo-electron microscopy. Proc Warl Acad Sei USA 1995, 92:10648-10652. Modelling of Fab atomic structures into cryoEM reconstructions of Sindbis Fab and Ross River-Fab complexes shows that the two monoclonal anti-bodies bind in slightly different orientations to identical locations on the E2 glycoproteins. These constitute the putative receptor binding sites for both viruses.
    • (1995) Proc Warl Acad Sei USA , vol.92 , pp. 10648-10652
    • Smith, T.J.1    Cheng, R.H.2    Olson, N.H.3    Peterson, P.4    Chase, E.5    Kuhn, R.J.6    Baker, T.S.7
  • 88
    • 0000677137 scopus 로고    scopus 로고
    • Principles of virus structure determination
    • Edited by Chiu W, Burnett RM, Garcea R. New York: Oxford University Press; in press
    • Baker TS, Johnson JE: Principles of virus structure determination. In Structural Biology of Viruses. Edited by Chiu W, Burnett RM, Garcea R. New York: Oxford University Press; 1996: in press.
    • (1996) Structural Biology of Viruses
    • Baker, T.S.1    Johnson, J.E.2
  • 90
    • 0030007379 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound bivalently to human rhinovirus 2
    • ̇̇92].
    • (1996) EMBO J , vol.15 , pp. 1515-1523
    • Hewat, E.A.1    Blaas, D.2
  • 91
    • 0029743275 scopus 로고    scopus 로고
    • Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon
    • in press
    • Smith TJ, Chase ES, Schmidt TJ, Oison NH, Baker TS: Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Nature 1996, in press. The first moderate resolution (4 Å) crystal structure of a virus-Fab complex reveals details of Fab-virus interactions. The pseudo-atomic model of HRV14-Fab 1 7IA [36,38] served as an initial phasing model for the X-ray crystallographic structure determination.
    • (1996) Nature
    • Smith, T.J.1    Chase, E.S.2    Schmidt, T.J.3    Oison, N.H.4    Baker, T.S.5
  • 93
    • 0029847931 scopus 로고    scopus 로고
    • Cryo-electron microscopy studies of empty capsids of human parvovirus B19, complexed with its cellular receptor
    • Chipman PR, Agbandje-McKenna M, Kajigaya S, Brown KE, Young NS, Baker TS, Rossmann MG: Cryo-electron microscopy studies of empty capsids of human parvovirus B19, complexed with its cellular receptor. Proc Natl Acad Sei USA 1996, 93:7502-7506. The second cryoEM reconstruction of a virus-receptor complex (compare with [40]). The glycolipid receptor molecules bind into depressions on the threefold axes of the B19-globoside complex. An atomic model of the tetrasaccharide component of the globoside receptor fits nicely into a difference map of the globoside density.
    • (1996) Proc Natl Acad Sei USA , vol.93 , pp. 7502-7506
    • Chipman, P.R.1    Agbandje-McKenna, M.2    Kajigaya, S.3    Brown, K.E.4    Young, N.S.5    Baker, T.S.6    Rossmann, M.G.7
  • 94
    • 0028874050 scopus 로고
    • The crystal structure of bluetongue virus VP7
    • Grimes J, Basak AK, Roy P, Stuart D: The crystal structure of bluetongue virus VP7. Nature 1995, 343:1 67-1 70. The 2.6 Å resolution structure of the VP7 subunit (349 amino acids) of blue tongue virus is determined by X-ray crystallography. A pseudo-atomic resolution model of the T=13 (780 subunits, 700 Å diameter) core of the virus is constructed by fitting the VP7 X-ray model to the 35 Å structure of the core, determined previously by cryoEM and image reconstruction.
    • (1995) Nature , vol.343 , pp. 167-170
    • Grimes, J.1    Basak, A.K.2    Roy, P.3    Stuart, D.4
  • 95
    • 0029143458 scopus 로고
    • Three-dimensional location of the main immunogenic region of the acetylcholine receptor
    • Beroukhim R, Unwin N: Three-dimensional location of the main immunogenic region of the acetylcholine receptor. Neuron 1995, 15:323-331.
    • (1995) Neuron , vol.15 , pp. 323-331
    • Beroukhim, R.1    Unwin, N.2


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