메뉴 건너뛰기




Volumn , Issue , 2011, Pages

Structural Biology Using Electrons and X-rays

(1)  Moody, Michael F a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85013689836     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/C2009-0-01500-1     Document Type: Book
Times cited : (3)

References (240)
  • 1
    • 60049098657 scopus 로고
    • Beitra die;ge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung
    • Abbe E. Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung. Arch. Mikr. Anat. 1873, 9:413-468.
    • (1873) Arch. Mikr. Anat. , vol.9 , pp. 413-468
    • Abbe, E.1
  • 2
    • 0003851729 scopus 로고
    • Washington, D.C., National Bureau of Standards, Applied Mathematics Series, 55. (Also reprinted by Dover Publications, New York.) [The National Institute of Standards and Technology, the Digital Library of Mathematical Functions; see .] (Eds.)
    • Abramowitz, M., Stegun, I.A. (Eds.), 1964. Handbook of Mathematical Functions with Formulas, Graphs, and Mathematical Tables, Washington, D.C., National Bureau of Standards, Applied Mathematics Series, 55. (Also reprinted by Dover Publications, New York.) [The National Institute of Standards and Technology, the Digital Library of Mathematical Functions; see .]. http://dlmf.nits.gov.
    • (1964) Handbook of Mathematical Functions with Formulas, Graphs, and Mathematical Tables
    • Abramowitz, M.1    Stegun, I.A.2
  • 6
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • Amos L.A., Henderson R., Unwin P.N.T. Three-dimensional structure determination by electron microscopy of two-dimensional crystals. Progr. Biophys. Mol. Biol. 1982, 39:183-231.
    • (1982) Progr. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.T.3
  • 7
    • 0000397743 scopus 로고
    • Chemical effects on nuclear induction signals from organic compounds
    • Arnold J.T., Dharmatti S.S., Packard M.E. Chemical effects on nuclear induction signals from organic compounds. J. Chem. Phys. 1951, 19:507.
    • (1951) J. Chem. Phys. , vol.19 , pp. 507
    • Arnold, J.T.1    Dharmatti, S.S.2    Packard, M.E.3
  • 8
    • 0006393051 scopus 로고
    • Two-dimensional spectroscopy. Application to nuclear magnetic resonance
    • Aue W.P., Bartholdi E., Ernst R.R. Two-dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 1976, 64(5):2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , Issue.5 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 9
    • 0020539720 scopus 로고
    • Polyoma virus 'hexamer' tubes consist of paired pentamers
    • Baker T.S., Caspar D.L.D., Murakami W.T. Polyoma virus 'hexamer' tubes consist of paired pentamers. Nature 1983, 303:446-448.
    • (1983) Nature , vol.303 , pp. 446-448
    • Baker, T.S.1    Caspar, D.L.D.2    Murakami, W.T.3
  • 10
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecule images by cryoelectron microscopy
    • Baker T.S., Cheng R.H. A model-based approach for determining orientations of biological macromolecule images 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
  • 11
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to viral life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • Baker T.S., Olson N.H., Fuller S.D. Adding the third dimension to viral life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol. Molec. Biol. Rev. 1999, 63:862-922.
    • (1999) Microbiol. Molec. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 13
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J.M., Henderson R. Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy 1984, 14:319-336.
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.M.1    Henderson, R.2
  • 14
    • 0024278917 scopus 로고
    • Images of purple membrane at 2.8 A ring; resolution obtained by cryo-electron microscopy
    • Baldwin J.M., Henderson R., Beckman E., Zemlin F. Images of purple membrane at 2.8 Å resolution obtained by cryo-electron microscopy. J. Mol. Biol. 1988, 202:585-591.
    • (1988) J. Mol. Biol. , vol.202 , pp. 585-591
    • Baldwin, J.M.1    Henderson, R.2    Beckman, E.3    Zemlin, F.4
  • 15
    • 84882085173 scopus 로고
    • I. Crystal symmetry. The actual basis of the thirty-two classes
    • Barlow W. I. Crystal symmetry. The actual basis of the thirty-two classes. Philosophical Magazine 1901, 1(6):1-36.
    • (1901) Philosophical Magazine , vol.1 , Issue.6 , pp. 1-36
    • Barlow, W.1
  • 18
    • 0001651415 scopus 로고
    • X-ray photographs of crystalline pepsin
    • Bernal J.D., Crowfoot D. X-ray photographs of crystalline pepsin. Nature 1934, 134:794-795.
    • (1934) Nature , vol.134 , pp. 794-795
    • Bernal, J.D.1    Crowfoot, D.2
  • 20
    • 0031460411 scopus 로고    scopus 로고
    • Distortion correction of tubular crystals: improvements in the acetylcholine receptor structure
    • Beroukhim R., Unwin N. Distortion correction of tubular crystals: improvements in the acetylcholine receptor structure. Ultramicroscopy 1997, 70:57-81.
    • (1997) Ultramicroscopy , vol.70 , pp. 57-81
    • Beroukhim, R.1    Unwin, N.2
  • 21
    • 0001510472 scopus 로고
    • The treatment of errors in the isomorphous replacement method
    • Blow D., Crick F.H.C. The treatment of errors in the isomorphous replacement method. Acta Crystallogr. 1959, 12:794-802.
    • (1959) Acta Crystallogr. , vol.12 , pp. 794-802
    • Blow, D.1    Crick, F.H.C.2
  • 23
    • 0024163316 scopus 로고
    • The reconstruction of helical particles with variable pitch
    • Bluemke D.A., Carragher B., Josephs R. The reconstruction of helical particles with variable pitch. Ultramicroscopy 1988, 26:255-270.
    • (1988) Ultramicroscopy , vol.26 , pp. 255-270
    • Bluemke, D.A.1    Carragher, B.2    Josephs, R.3
  • 24
    • 0001509820 scopus 로고
    • Fourier synthesis of the crystal structure of strychnine sulphate pentahydrate
    • Bokhoven C., Schoone J.C., Bijvoet J.M. Fourier synthesis of the crystal structure of strychnine sulphate pentahydrate. Acta Crystallogr. 1951, 5:275-280.
    • (1951) Acta Crystallogr. , vol.5 , pp. 275-280
    • Bokhoven, C.1    Schoone, J.C.2    Bijvoet, J.M.3
  • 26
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 27
    • 0024688345 scopus 로고
    • The Fourier transform
    • Bracewell R.N. The Fourier transform. Sci. Am. 1989, 260(6):62-69.
    • (1989) Sci. Am. , vol.260 , Issue.6 , pp. 62-69
    • Bracewell, R.N.1
  • 29
    • 0002493672 scopus 로고
    • The diffraction of short electromagnetic waves by a crystal
    • Bragg W.L. The diffraction of short electromagnetic waves by a crystal. Proc. Cambridge Phil. Soc. 1914, 17:43-57.
    • (1914) Proc. Cambridge Phil. Soc. , vol.17 , pp. 43-57
    • Bragg, W.L.1
  • 30
    • 30444453146 scopus 로고
    • X-ray analysis with the aid of the 'fly's eye
    • Bragg W.L., Stokes A.R. X-ray analysis with the aid of the 'fly's eye. Nature 1945, 156:332-333.
    • (1945) Nature , vol.156 , pp. 332-333
    • Bragg, W.L.1    Stokes, A.R.2
  • 31
  • 32
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner S., Horne R.W. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta 1959, 34:103-110.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 33
    • 33746368163 scopus 로고    scopus 로고
    • Fourier transforms in crystallography: theory, algorithms and applications (Chap. 1.3)
    • Kluwer Academic Publishers, Dordrecht, The Netherlands for the International Union of Crystallography
    • Bricogne G. Fourier transforms in crystallography: theory, algorithms and applications (Chap. 1.3). International Tables for Crystallography, Reciprocal Space 2001, vol. B:25-98. Kluwer Academic Publishers, Dordrecht, The Netherlands for the International Union of Crystallography.
    • (2001) International Tables for Crystallography, Reciprocal Space , vol.B , pp. 25-98
    • Bricogne, G.1
  • 35
    • 0021723207 scopus 로고
    • Tubular crystals of acetylcholine receptor
    • Brisson A., Unwin P.N.T. Tubular crystals of acetylcholine receptor. J. Cell Biol. 1984, 99:1202-1211.
    • (1984) J. Cell Biol. , vol.99 , pp. 1202-1211
    • Brisson, A.1    Unwin, P.N.T.2
  • 37
    • 0023206468 scopus 로고
    • Use of spot-scan procedure for recording low-dose images of beam-sensitive specimens
    • Bullough P., Henderson R. Use of spot-scan procedure for recording low-dose images of beam-sensitive specimens. Ultramicroscopy 1987, 21(3):223-230.
    • (1987) Ultramicroscopy , vol.21 , Issue.3 , pp. 223-230
    • Bullough, P.1    Henderson, R.2
  • 38
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: the role of mechanics at the molecular level
    • Calladine C.R. Change of waveform in bacterial flagella: the role of mechanics at the molecular level. J. Mol. Biol. 1978, 118:457-479.
    • (1978) J. Mol. Biol. , vol.118 , pp. 457-479
    • Calladine, C.R.1
  • 39
    • 0037282736 scopus 로고    scopus 로고
    • The variance of icosahedral virus models is a key indicator in the structure determination: a model-free reconstruction of viruses, suitable for refractory particles
    • Cantele F., Lanzavecchia S., Bellon P.L. The variance of icosahedral virus models is a key indicator in the structure determination: a model-free reconstruction of viruses, suitable for refractory particles. J. Struct. Biol. 2003, 141:84-92.
    • (2003) J. Struct. Biol. , vol.141 , pp. 84-92
    • Cantele, F.1    Lanzavecchia, S.2    Bellon, P.L.3
  • 40
    • 36949079814 scopus 로고
    • Structure of bushy stunt virus
    • Caspar D.L.D. Structure of bushy stunt virus. Nature 1956, 177:4756.
    • (1956) Nature , vol.177 , pp. 4756
    • Caspar, D.L.D.1
  • 42
    • 0025312416 scopus 로고
    • Analysis of high-resolution electron diffraction patterns from purple membrane labelled with heavy-atoms
    • Ceska T.A., Henderson R. Analysis of high-resolution electron diffraction patterns from purple membrane labelled with heavy-atoms. J. Mol. Biol. 1990, 213:539-560.
    • (1990) J. Mol. Biol. , vol.213 , pp. 539-560
    • Ceska, T.A.1    Henderson, R.2
  • 44
    • 49349112116 scopus 로고    scopus 로고
    • Subnanometer-resolution structures of the grass carp reovirus core and virion
    • Cheng L., Fang Q., Shah S., Atanasov I.C., Zhou Z.H. Subnanometer-resolution structures of the grass carp reovirus core and virion. J. Mol. Biol. 2008, 382:213-222.
    • (2008) J. Mol. Biol. , vol.382 , pp. 213-222
    • Cheng, L.1    Fang, Q.2    Shah, S.3    Atanasov, I.C.4    Zhou, Z.H.5
  • 45
    • 84882112642 scopus 로고    scopus 로고
    • Icosahedral particles
    • Chapter 13 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • Chiu, W., 2007. Icosahedral particles. Chapter 13 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • (2007)
    • Chiu, W.1
  • 46
    • 0035919727 scopus 로고    scopus 로고
    • Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination
    • Clemons W.M., Broderson D.E., McCutcheon J.P., May J.L., Carter A.P., Morgan-Warren R.J., et al. Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: purification, crystallization and structure determination. J. Mol. Biol. 2001, 310:827-843.
    • (2001) J. Mol. Biol. , vol.310 , pp. 827-843
    • Clemons, W.M.1    Broderson, D.E.2    McCutcheon, J.P.3    May, J.L.4    Carter, A.P.5    Morgan-Warren, R.J.6
  • 47
    • 0001704671 scopus 로고
    • The structure of synthetic polypeptides. I. The transform of atoms on a helix
    • Cochran W., Crick F.H.C., Vand V. The structure of synthetic polypeptides. I. The transform of atoms on a helix. Acta Crystallogr. 1952, 5:581-586.
    • (1952) Acta Crystallogr. , vol.5 , pp. 581-586
    • Cochran, W.1    Crick, F.H.C.2    Vand, V.3
  • 48
    • 0043175614 scopus 로고
    • The spherical harmonics with the symmetry of the icosahedral group
    • Cohan N.V. The spherical harmonics with the symmetry of the icosahedral group. Proc. Cambridge Phil. Soc. 1958, 54:28-38.
    • (1958) Proc. Cambridge Phil. Soc. , vol.54 , pp. 28-38
    • Cohan, N.V.1
  • 49
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J., Cheng N., Wingfield P.T., Stahl S.J., Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 1997, 386:91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.1    Cheng, N.2    Wingfield, P.T.3    Stahl, S.J.4    Steven, A.C.5
  • 50
    • 84968470212 scopus 로고
    • An algorithm for the machine calculation of complex Fourier series
    • Cooley J.W., Tukey J.W. An algorithm for the machine calculation of complex Fourier series. Math. Comput. 1965, 19:297-301.
    • (1965) Math. Comput. , vol.19 , pp. 297-301
    • Cooley, J.W.1    Tukey, J.W.2
  • 52
    • 85051698193 scopus 로고    scopus 로고
    • Electron diffraction and electron microscopy
    • Kluwer Academic Publishers, Dordrecht, The Netherlands, for the International Union of Crystallography, Chap 2.5.2
    • Cowley J.M. Electron diffraction and electron microscopy. International Tables for Crystallography, Reciprocal Space 2001, vol. B:277-285. Kluwer Academic Publishers, Dordrecht, The Netherlands, for the International Union of Crystallography, Chap 2.5.2.
    • (2001) International Tables for Crystallography, Reciprocal Space , vol.B , pp. 277-285
    • Cowley, J.M.1
  • 54
    • 0019728251 scopus 로고
    • Reconstruction of imperfectly ordered zinc-induced tubulin sheets using cross-correlation and real space averaging
    • Crepeau R.H., Fram E.K. Reconstruction of imperfectly ordered zinc-induced tubulin sheets using cross-correlation and real space averaging. Ultramicroscopy 1981, 6:7-17.
    • (1981) Ultramicroscopy , vol.6 , pp. 7-17
    • Crepeau, R.H.1    Fram, E.K.2
  • 55
    • 84882112875 scopus 로고
    • Ph.D Thesis, Cambridge University.
    • Crick, F.H.C, 1953. Ph.D. Thesis, Cambridge University.
    • (1953)
    • Crick, F.H.C.1
  • 56
    • 36949077319 scopus 로고
    • The structure of small viruses
    • Crick F.H.C., Watson J.D. The structure of small viruses. Nature 1956, 177:473-475.
    • (1956) Nature , vol.177 , pp. 473-475
    • Crick, F.H.C.1    Watson, J.D.2
  • 57
    • 0014930077 scopus 로고
    • Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A., Amos L.A., Finch J.T., DeRosier D.J. Three-dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature 1970, 226:421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    DeRosier, D.J.4
  • 58
    • 0014894609 scopus 로고
    • The reconstruction of three-dimensional structure from projections and its application to electron microscopy
    • Crowther R.A., DeRosier D.J., Klug A. The reconstruction of three-dimensional structure from projections and its application to electron microscopy. Proc. Roy. Soc. Lond. A 1970, 317:319-340.
    • (1970) Proc. Roy. Soc. Lond. A , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 59
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. Lond., B 1971, 261:221-230.
    • (1971) Phil. Trans. Roy. Soc. Lond., B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 60
    • 0015243520 scopus 로고
    • Harmonic analysis of electron microscope images with rotational symmetry
    • Crowther R.A., Amos L.A. Harmonic analysis of electron microscope images with rotational symmetry. J. Mol. Biol. 1971, 60:123-130.
    • (1971) J. Mol. Biol. , vol.60 , pp. 123-130
    • Crowther, R.A.1    Amos, L.A.2
  • 61
    • 0003711494 scopus 로고
    • M.G. (Ed.), The Molecular Replacement Method. Gordon & Breach, New York, R.A. Crowther (Ed.)
    • Crowther R.A. In: Rossmann 1972, 173-178. M.G. (Ed.), The Molecular Replacement Method. Gordon & Breach, New York. R.A. Crowther (Ed.).
    • (1972) In: Rossmann , pp. 173-178
    • Crowther, R.A.1
  • 62
    • 0017576943 scopus 로고
    • An analysis of the fine structure of surface layers from two strains of Clostridia, including correction for distorted images
    • Crowther R.A., Sleytr U.B. An analysis of the fine structure of surface layers from two strains of Clostridia, including correction for distorted images. J. Ultrastr. Res. 1977, 58:41-49.
    • (1977) J. Ultrastr. Res. , vol.58 , pp. 41-49
    • Crowther, R.A.1    Sleytr, U.B.2
  • 63
    • 0022419384 scopus 로고
    • Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle
    • Crowther R.A., Padron R., Craig R. Arrangement of the heads of myosin in relaxed thick filaments from tarantula muscle. J. Mol. Biol. 1985, 184:429-439.
    • (1985) J. Mol. Biol. , vol.184 , pp. 429-439
    • Crowther, R.A.1    Padron, R.2    Craig, R.3
  • 64
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther R.A., Kiselev N.A., Böttcher B., Berriman J.A., Borisova G.P., Ose V., et al. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 1994, 77:943-950.
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6
  • 66
    • 45249115226 scopus 로고    scopus 로고
    • Microscopy goes cold: frozen viruses reveal their structural secrets. (The Leeuwenhoek lecture 2006.)
    • Crowther R.A. Microscopy goes cold: frozen viruses reveal their structural secrets. (The Leeuwenhoek lecture 2006.). Phil. Trans. R. Soc. B 2008, 363:2441-2451.
    • (2008) Phil. Trans. R. Soc. B , vol.363 , pp. 2441-2451
    • Crowther, R.A.1
  • 67
    • 0000668797 scopus 로고
    • Reconstruction of three dimensional structures from electron micrographs
    • DeRosier D.J., Klug A. Reconstruction of three dimensional structures from electron micrographs. Nature 1968, 217:130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 68
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional Images from electron micrographs of structures with helical symmetry
    • DeRosier D.J., Moore P.B. Reconstruction of three-dimensional Images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 1970, 52:355-369.
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • DeRosier, D.J.1    Moore, P.B.2
  • 69
    • 84882152675 scopus 로고    scopus 로고
    • Electron crystallography of helical structures
    • Chapter 12 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • DeRosier, D.J., 2007. Electron crystallography of helical structures. Chapter 12 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • (2007)
    • DeRosier, D.J.1
  • 71
    • 0022929708 scopus 로고
    • Improvement in high-resolution image quality of radiation sensitive specimens achieved with reduced spot size of the electron beam
    • Downing K.H., Glaeser R.M. Improvement in high-resolution image quality of radiation sensitive specimens achieved with reduced spot size of the electron beam. Ultramicroscopy 1986, 20:269-278.
    • (1986) Ultramicroscopy , vol.20 , pp. 269-278
    • Downing, K.H.1    Glaeser, R.M.2
  • 72
    • 0027418576 scopus 로고
    • The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry
    • Dube P., Tavares P., Lurz R., Heel M. van The portal protein of bacteriophage SPP1: a DNA pump with 13-fold symmetry. EMBO J. 1993, 12:1303-1309.
    • (1993) EMBO J. , vol.12 , pp. 1303-1309
    • Dube, P.1    Tavares, P.2    Lurz, R.3    Heel, M.4
  • 76
    • 0022928662 scopus 로고
    • An algorithm for straightening images of curved filamentous structures
    • Egelman E.H. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy 1986, 19:367-373.
    • (1986) Ultramicroscopy , vol.19 , pp. 367-373
    • Egelman, E.H.1
  • 77
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single particle methods. Ultramicroscopy 2000, 85:225-234.
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 78
    • 0002521965 scopus 로고
    • Application of Fourier Transform spectroscopy to magnetic resonance
    • Ernst R.R., Anderson W.A. Application of Fourier Transform spectroscopy to magnetic resonance. Rev. Sci. Instrum. 1966, 37:93-102.
    • (1966) Rev. Sci. Instrum. , vol.37 , pp. 93-102
    • Ernst, R.R.1    Anderson, W.A.2
  • 81
    • 0001753477 scopus 로고
    • Structural studies of viruses
    • Academic Press, New York and London
    • Finch J.T., Holmes K.C. Structural studies of viruses. Methods in Virology 1967, vol. III:351-474. Academic Press, New York and London.
    • (1967) Methods in Virology , vol.3 , pp. 351-474
    • Finch, J.T.1    Holmes, K.C.2
  • 82
    • 0025286635 scopus 로고
    • Classification of macromolecular assemblies studied as 'single particles'
    • Frank J. Classification of macromolecular assemblies studied as 'single particles'. Quart. Rev. Biophysics 1990, 23:281-329.
    • (1990) Quart. Rev. Biophysics , vol.23 , pp. 281-329
    • Frank, J.1
  • 83
    • 0027541853 scopus 로고
    • Flopping polypeptide chains and Suleika's subtle imperfections: analysis of variations in the electron micrograph of a purple membrane crystal
    • Frank J., Chiu W., Henderson R. Flopping polypeptide chains and Suleika's subtle imperfections: analysis of variations in the electron micrograph of a purple membrane crystal. Ultramicroscopy 1993, 49:387-396.
    • (1993) Ultramicroscopy , vol.49 , pp. 387-396
    • Frank, J.1    Chiu, W.2    Henderson, R.3
  • 85
    • 84882156600 scopus 로고    scopus 로고
    • Single particles
    • Chapter 14 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • Frank, J., 2007. Single particles. Chapter 14 of Glaeser et al. (2007) Electron Crystallography of Biological Macromolecules. New York: Oxford University Press.
    • (2007)
    • Frank, J.1
  • 86
    • 0000146734 scopus 로고
    • The splitting of layer lines in X-ray fibre diagrams of helical structures: application to tobacco mosaic virus
    • Franklin R.E., Klug A. The splitting of layer lines in X-ray fibre diagrams of helical structures: application to tobacco mosaic virus. Acta Crystallogr. 1955, 8:777-781.
    • (1955) Acta Crystallogr. , vol.8 , pp. 777-781
    • Franklin, R.E.1    Klug, A.2
  • 87
    • 0006757280 scopus 로고
    • Tobacco mosaic virus: application of the method of isomorphous replacement to the determination of the helical parameters and radial density distribution
    • Franklin R.E., Holmes K.C. Tobacco mosaic virus: application of the method of isomorphous replacement to the determination of the helical parameters and radial density distribution. Acta. Crystallogr. 1958, 11:213-220.
    • (1958) Acta. Crystallogr. , vol.11 , pp. 213-220
    • Franklin, R.E.1    Holmes, K.C.2
  • 88
    • 11444253481 scopus 로고    scopus 로고
    • Breaking the spherical and chromatic aberration barrier in transmission electron microscopy
    • Freitag B., Kujawa S., Mul U., Ringuelda J., Tiemeijer P.C. Breaking the spherical and chromatic aberration barrier in transmission electron microscopy. Ultramicroscopy 2005, 102:209-214.
    • (2005) Ultramicroscopy , vol.102 , pp. 209-214
    • Freitag, B.1    Kujawa, S.2    Mul, U.3    Ringuelda, J.4    Tiemeijer, P.C.5
  • 89
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid
    • Fuller S.D. The T=4 envelope of Sindbis virus is organized by interactions with a complementary T=3 capsid. Cell 1987, 48:923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 90
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles - the uncommon line
    • Fuller S.D., Butcher S.J., Cheng R.H., Baker T.S. Three-dimensional reconstruction of icosahedral particles - the uncommon line. J. Struct. Biol. 1996, 116:48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 92
    • 0015523343 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy. II. Direct methods
    • Gilbert P.F.C. The reconstruction of a three-dimensional structure from projections and its application to electron microscopy. II. Direct methods. Proc. Roy. Soc. Lond. B 1972, 182:89-102.
    • (1972) Proc. Roy. Soc. Lond. B , vol.182 , pp. 89-102
    • Gilbert, P.F.C.1
  • 93
    • 0017873876 scopus 로고
    • Radiation damage related to transmission electron microscopy of biological specimens at low temperatures: a review
    • Glaeser R.M., Taylor K.A. Radiation damage related to transmission electron microscopy of biological specimens at low temperatures: a review. J. Microsc. 1978, 112:127-138.
    • (1978) J. Microsc. , vol.112 , pp. 127-138
    • Glaeser, R.M.1    Taylor, K.A.2
  • 96
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen T., Sliz P., Kistler J., Cheng Y., Walz T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 2004, 429:193-197.
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 97
    • 0004080484 scopus 로고
    • Roberts & Company, Englewood, Colorado, (Earlier editions: San Francisco: McGraw-Hill Book Company.)
    • Goodman J.W. Introduction to Fourier Optics 1968-2004, Roberts & Company, Englewood, Colorado, (Earlier editions: San Francisco: McGraw-Hill Book Company.). third ed.
    • (1968) Introduction to Fourier Optics
    • Goodman, J.W.1
  • 98
    • 0014905513 scopus 로고
    • Algebraic reconstruction techniques (ART) for three-dimensional electron microscopy and X-ray photography
    • Gordon R., Bender R., Herman G.T. Algebraic reconstruction techniques (ART) for three-dimensional electron microscopy and X-ray photography. J. Theor. Biol. 1970, 29:471-481.
    • (1970) J. Theor. Biol. , vol.29 , pp. 471-481
    • Gordon, R.1    Bender, R.2    Herman, G.T.3
  • 99
    • 0001262916 scopus 로고
    • Structure of haemoglobin IV: sign determination by the isomorphous replacement method
    • Green D.W., Ingram V.M., Perutz M.F. Structure of haemoglobin IV: sign determination by the isomorphous replacement method. Proc. Roy. Soc. Lond. A 1954, 225:287-307.
    • (1954) Proc. Roy. Soc. Lond. A , vol.225 , pp. 287-307
    • Green, D.W.1    Ingram, V.M.2    Perutz, M.F.3
  • 101
    • 0038569732 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, Dordrecht, The Netherlands, for the International Union of Crystallography
    • International Tables for Crystallography: Space-group symmetry 2002, vol. A. Kluwer Academic Publishers, Dordrecht, The Netherlands, for the International Union of Crystallography. fifth ed.
    • (2002) International Tables for Crystallography: Space-group symmetry , vol.A
  • 102
    • 85019291339 scopus 로고
    • Electron densitometry of stained virus particles
    • Hall C.E. Electron densitometry of stained virus particles. J. Biophys. Biochem. Cytol. 1955, 1:1-12.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 1-12
    • Hall, C.E.1
  • 104
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz G., van Heel M. Exact filters for general geometry three dimensional reconstruction. Optik 1986, 73:146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 105
    • 0004247764 scopus 로고    scopus 로고
    • Yale University Press, New Haven & London
    • Harris H. The Birth of the Cell 1999, Yale University Press, New Haven & London.
    • (1999) The Birth of the Cell
    • Harris, H.1
  • 106
    • 36149002730 scopus 로고
    • Receptor mechanisms and the integration of sensory information in the eye
    • New York
    • Hartline, H.K., 1959. Receptor mechanisms and the integration of sensory information in the eye. In: Biophysical Sciences - A Study Program. J. Wiley, New York, pp. 515-523.
    • (1959) Biophysical Sciences - A Study Program. J. Wiley , pp. 515-523
    • Hartline, H.K.1
  • 107
    • 0020293428 scopus 로고
    • Design and operation of cold stages
    • Heide H.G. Design and operation of cold stages. Ultramicroscopy 1982, 10:125-154.
    • (1982) Ultramicroscopy , vol.10 , pp. 125-154
    • Heide, H.G.1
  • 109
    • 0000895319 scopus 로고
    • The difference Fourier technique in protein crystallography: errors and their treatment
    • Henderson R., Moffat J.K. The difference Fourier technique in protein crystallography: errors and their treatment. Acta Cryst. B 1971, 27:1414-1420.
    • (1971) Acta Cryst. B , vol.27 , pp. 1414-1420
    • Henderson, R.1    Moffat, J.K.2
  • 110
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N.T. 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
  • 111
    • 0021786909 scopus 로고
    • Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals
    • Henderson R., Glaeser R.M. Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals. Ultramicroscopy 1985, 16:139-150.
    • (1985) Ultramicroscopy , vol.16 , pp. 139-150
    • Henderson, R.1    Glaeser, R.M.2
  • 112
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 A ring; resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., Zemlin F. Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 113
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. 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
  • 114
    • 0026523919 scopus 로고
    • Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice
    • Henderson R. Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicroscopy 1992, 46:1-18.
    • (1992) Ultramicroscopy , vol.46 , pp. 1-18
    • Henderson, R.1
  • 115
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules
    • Henderson R. The potential and limitations of neutrons, electrons and X-rays for atomic-resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 1995, 28:171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 116
    • 3142655417 scopus 로고    scopus 로고
    • Realizing the potential of electron cryo-microscopy
    • Henderson R. Realizing the potential of electron cryo-microscopy. Q. Rev. Biophys. 2004, 37:3-13.
    • (2004) Q. Rev. Biophys. , vol.37 , pp. 3-13
    • Henderson, R.1
  • 118
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Güntert P., Wüthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 2002, 319:209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 120
    • 84882212077 scopus 로고    scopus 로고
    • Principles of membrane protein interactions with annular lipids deduced from aquaporin-O 2D crystals
    • (13 April 2010)
    • Hite R.K., Li Z., Walz T. Principles of membrane protein interactions with annular lipids deduced from aquaporin-O 2D crystals. EMBO J. 2010, 1-7. (13 April 2010).
    • (2010) EMBO J. , pp. 1-7
    • Hite, R.K.1    Li, Z.2    Walz, T.3
  • 121
    • 0015354409 scopus 로고
    • Determination of heavy atom positions in tobacco mosaic virus from double heavy atom derivatives
    • Holmes K.C., Mandelkow E., Leigh J.B. Determination of heavy atom positions in tobacco mosaic virus from double heavy atom derivatives. Naturwiss 1972, 59:247-254.
    • (1972) Naturwiss , vol.59 , pp. 247-254
    • Holmes, K.C.1    Mandelkow, E.2    Leigh, J.B.3
  • 122
    • 84944000693 scopus 로고
    • Point groups and plane groups in a two-sided plane and their sub-groups
    • Holser W.T. Point groups and plane groups in a two-sided plane and their sub-groups. Z. Kristallogr. 1958, 110:268-281.
    • (1958) Z. Kristallogr. , vol.110 , pp. 268-281
    • Holser, W.T.1
  • 124
    • 58149421595 scopus 로고
    • Analysis of a complex of statistical variables into principal components
    • 498-520
    • Hotelling H. Analysis of a complex of statistical variables into principal components. J. Educ. Psychol. 1933, 24:417-441. & 498-520.
    • (1933) J. Educ. Psychol. , vol.24 , pp. 417-441
    • Hotelling, H.1
  • 126
    • 0742317562 scopus 로고
    • Some observations on the structure of tobacco mosaic virus
    • Almquist & Wiksell, Stockholm, pp. 260-261
    • Huxley H.E. Some observations on the structure of tobacco mosaic virus. Proceedings of the Stockholm Conference on Electron Microscopy 1956, Almquist & Wiksell, Stockholm, pp. 260-261.
    • (1956) Proceedings of the Stockholm Conference on Electron Microscopy
    • Huxley, H.E.1
  • 127
    • 0014414249 scopus 로고
    • Structural difference between resting and rigor muscle; evidence from intensity changes in the low-angle equatorial X-ray diagram
    • Huxley H.E. Structural difference between resting and rigor muscle; evidence from intensity changes in the low-angle equatorial X-ray diagram. J. Mol. Biol. 1968, 37:507-520.
    • (1968) J. Mol. Biol. , vol.37 , pp. 507-520
    • Huxley, H.E.1
  • 130
    • 0024961660 scopus 로고
    • Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy
    • Jeng T.-W., Crowther R.A., Stubbs G., Chiu W. Visualization of alpha-helices 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    Chiu, W.4
  • 131
    • 84882053708 scopus 로고    scopus 로고
    • Cryo-electron microscopy of isosahedral virus particles
    • Humana Press, N.J, J. Kui (Ed.)
    • Jiang W., Chiu W. Cryo-electron microscopy of isosahedral virus particles. Methods in Molecular Biology 2006, Humana Press, N.J. J. Kui (Ed.).
    • (2006) Methods in Molecular Biology
    • Jiang, W.1    Chiu, W.2
  • 133
    • 0042756489 scopus 로고
    • Study of single crystals and their associations in polymers
    • Keller A., O'Connor A. Study of single crystals and their associations in polymers. Disc. Farad. Soc. 1958, 25:114.
    • (1958) Disc. Farad. Soc. , vol.25 , pp. 114
    • Keller, A.1    O'Connor, A.2
  • 136
    • 0014674281 scopus 로고
    • The structure of viruses of the papilloma-polyoma type. V. Tubular variants built of pentamers
    • Kiselev N.A., Klug A. The structure of viruses of the papilloma-polyoma type. V. Tubular variants built of pentamers. J. Mol. Biol. 1969, 40:155-171.
    • (1969) J. Mol. Biol. , vol.40 , pp. 155-171
    • Kiselev, N.A.1    Klug, A.2
  • 138
    • 0007797760 scopus 로고
    • An optical method for the analysis of periodicities in electron micrographs, and some observations on the mechanism of negative straining
    • Klug A., Berger J.E. An optical method for the analysis of periodicities in electron micrographs, and some observations on the mechanism of negative straining. J. Mol. Biol. 1964, 10:505-569.
    • (1964) J. Mol. Biol. , vol.10 , pp. 505-569
    • Klug, A.1    Berger, J.E.2
  • 139
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W., Wang D.N., 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
  • 140
    • 0017127543 scopus 로고
    • Ribosome structure determined by electron microscopy of Escherichia coli small subunits, large subunits and monomeric subunits
    • Lake J.A. Ribosome structure determined by electron microscopy of Escherichia coli small subunits, large subunits and monomeric subunits. J. Mol. Biol. 1976, 105:131-159.
    • (1976) J. Mol. Biol. , vol.105 , pp. 131-159
    • Lake, J.A.1
  • 141
    • 0041984985 scopus 로고
    • Anwendung des Bilddifferenzverfarhrens auf die Untersuchung von Struktura die;nderungen du die;nner Kohlefolien bei Elektronenbestrahlung
    • Langer R., Frank J., Feltynowski A., Hopoe W. Anwendung des Bilddifferenzverfarhrens auf die Untersuchung von Strukturänderungen dünner Kohlefolien bei Elektronenbestrahlung. Ber. Bunsenges. Phys. Chem. 1970, 74:1120-1126.
    • (1970) Ber. Bunsenges. Phys. Chem. , vol.74 , pp. 1120-1126
    • Langer, R.1    Frank, J.2    Feltynowski, A.3    Hopoe, W.4
  • 146
    • 37349116067 scopus 로고    scopus 로고
    • Symmetry-adapted spherical harmonics method for high-resolution 3D single-particle reconstructions
    • Liu H., Cheng L., Zeng X., Cai C., Zhou Z.H., Yang Q. Symmetry-adapted spherical harmonics method for high-resolution 3D single-particle reconstructions. J. Struct. Biol. 2008, 161:64-73.
    • (2008) J. Struct. Biol. , vol.161 , pp. 64-73
    • Liu, H.1    Cheng, L.2    Zeng, X.3    Cai, C.4    Zhou, Z.H.5    Yang, Q.6
  • 147
    • 0001207563 scopus 로고
    • Resolution d'un structure crystalline lorsque les positions d'une partie des atoms sont connues: traitement statistique
    • Luzzati V. Resolution d'un structure crystalline lorsque les positions d'une partie des atoms sont connues: traitement statistique. Acta Crystallogr. 1953, 6:142-152.
    • (1953) Acta Crystallogr. , vol.6 , pp. 142-152
    • Luzzati, V.1
  • 148
    • 0002512329 scopus 로고
    • Methods for the enhancement of image detail and accentuation of structure in electron microscopy
    • Markham R., Frey S., Hills G.J. Methods for the enhancement of image detail and accentuation of structure in electron microscopy. Virology 1963, 20:88-102.
    • (1963) Virology , vol.20 , pp. 88-102
    • Markham, R.1    Frey, S.2    Hills, G.J.3
  • 151
    • 17744384377 scopus 로고
    • On the transformation of surfaces by bending
    • (Reprinted, 1890, in The Scientific Papers of J.C. Maxell, 1, ed. W.D. Niven, 81-114. University Press, Cambridge.)
    • Maxwell J.C. On the transformation of surfaces by bending. Cambridge Phil. Soc. Trans. 1854, 9:455-469. (Reprinted, 1890, in The Scientific Papers of J.C. Maxell, vol. 1, ed. W.D. Niven, pp. 81-114. University Press, Cambridge.).
    • (1854) Cambridge Phil. Soc. Trans. , vol.9 , pp. 455-469
    • Maxwell, J.C.1
  • 153
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 A ring; resolution based on electron crystallography: implication of the charge distribution
    • Mitsuoka K., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., et al. The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol. 1999, 286:861-882.
    • (1999) J. Mol. Biol. , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6
  • 154
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 A ring; resolution: transverse channels in the channel wall
    • Miyazawa A., Fuyiyoshi Y., Stowell M., Unwin N. Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse channels in the channel wall. J. Mol. Biol. 1999, 288:765-786.
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fuyiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 155
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fuyiyoshi Y., Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 2003, 423:949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fuyiyoshi, Y.2    Unwin, N.3
  • 156
    • 0001267296 scopus 로고
    • The shape of the T-even bacteriophage head
    • Moody M.F. The shape of the T-even bacteriophage head. Virology 1965, 26:567-576.
    • (1965) Virology , vol.26 , pp. 567-576
    • Moody, M.F.1
  • 157
    • 0014219440 scopus 로고
    • Structure of the sheath of bacteriophage T4. I. Structure of the contracted sheath and polysheath
    • Moody M.F. Structure of the sheath of bacteriophage T4. I. Structure of the contracted sheath and polysheath. J. Mol. Biol. 1967, 24:167-200.
    • (1967) J. Mol. Biol. , vol.24 , pp. 167-200
    • Moody, M.F.1
  • 158
    • 0015867079 scopus 로고
    • Structure of the sheath of bacteriophage T4. III. Contraction mechanism deduced from partially contracted sheaths
    • Moody M.F. Structure of the sheath of bacteriophage T4. III. Contraction mechanism deduced from partially contracted sheaths. J. Mol. Biol. 1973, 80:613-635.
    • (1973) J. Mol. Biol. , vol.80 , pp. 613-635
    • Moody, M.F.1
  • 159
    • 0003056635 scopus 로고
    • Image analysis of electron micrographs
    • Academic Press, London, P.W. Hawkes, U. Valdrè (Eds.)
    • Moody M.F. Image analysis of electron micrographs. Biophysical Electron Microscopy 1990, 145-287. Academic Press, London. P.W. Hawkes, U. Valdrè (Eds.).
    • (1990) Biophysical Electron Microscopy , pp. 145-287
    • Moody, M.F.1
  • 160
    • 0032727550 scopus 로고    scopus 로고
    • Geometry of phage head construction
    • Moody M.F. Geometry of phage head construction. J. Mol. Biol. 1999, 293:401-429.
    • (1999) J. Mol. Biol. , vol.293 , pp. 401-429
    • Moody, M.F.1
  • 161
    • 0022518526 scopus 로고
    • Structure of tobacco mosaic virus at 3.6 A ring; resolution: implications for assembly
    • Namba K., Stubbs G. Structure of tobacco mosaic virus at 3.6 Å resolution: implications for assembly. Science 1986, 231:1401-1406.
    • (1986) Science , vol.231 , pp. 1401-1406
    • Namba, K.1    Stubbs, G.2
  • 163
    • 0344552376 scopus 로고    scopus 로고
    • On the three-dimensional reconstruction of icosahedral particles
    • Navaza J. On the three-dimensional reconstruction of icosahedral particles. J. Struct. Biol. 2003, 144:13-23.
    • (2003) J. Struct. Biol. , vol.144 , pp. 13-23
    • Navaza, J.1
  • 164
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha; beta; tubulin dimer by electron crystallography
    • Nogales E., Wolf S., Downing K.H. Structure of the αβ tubulin dimer by electron crystallography. Nature 1998, 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.2    Downing, K.H.3
  • 166
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D., Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 1971, 233:149-152.
    • (1971) Nature New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 167
    • 0001598843 scopus 로고
    • A direct method for the determination of the components of interatomic distances in crystals
    • Patterson A.L. A direct method for the determination of the components of interatomic distances in crystals. Z. Kristallogr. 1935, 90:517-542.
    • (1935) Z. Kristallogr. , vol.90 , pp. 517-542
    • Patterson, A.L.1
  • 168
    • 76549252207 scopus 로고
    • The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L., Corey R.B., Branson H.R. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Nat. Acad. Sci. USA 1951, 37:205-211.
    • (1951) Proc. Nat. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 169
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P.A., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 1992, 40:33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.A.1    Radermacher, M.2    Frank, J.3
  • 171
    • 0024250191 scopus 로고
    • Three-dimensional reconstruction from electron micrographs of disordered specimens. I. Method
    • Provencher S.W., Vogel R.H. Three-dimensional reconstruction from electron micrographs of disordered specimens. I. Method. Ultramicroscopy 1988, 25:209-222.
    • (1988) Ultramicroscopy , vol.25 , pp. 209-222
    • Provencher, S.W.1    Vogel, R.H.2
  • 172
    • 0024220731 scopus 로고
    • Three-dimensional reconstruction from electron micrographs of disordered specimens. II. Implementation and results
    • Provencher S.W., Vogel R.H. Three-dimensional reconstruction from electron micrographs of disordered specimens. II. Implementation and results. Ultramicroscopy 1988, 25:223-240.
    • (1988) Ultramicroscopy , vol.25 , pp. 223-240
    • Provencher, S.W.1    Vogel, R.H.2
  • 173
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M., Wagenknecht T., Verschoor A., Frank J. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 1987, 146:113-136.
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 174
    • 0001339881 scopus 로고
    • Three-dimensional reconstruction of single particles from random and non-random tilt series
    • Radermacher M. Three-dimensional reconstruction of single particles from random and non-random tilt series. J. Elect. Microsc. Tech. 1988, 9:359-394.
    • (1988) J. Elect. Microsc. Tech. , vol.9 , pp. 359-394
    • Radermacher, M.1
  • 175
    • 0001169360 scopus 로고
    • U die;ber die Bestimmung von Funktionen durch ihre Integralwerte la die;ngs gewisser Mannigfaltigkeiten
    • Radon J. Über die Bestimmung von Funktionen durch ihre Integralwerte längs gewisser Mannigfaltigkeiten. Ber. Sachs. Akad. Wiss. Leipzig. Kl. 1917, 69:262-277.
    • (1917) Ber. Sachs. Akad. Wiss. Leipzig. Kl. , vol.69 , pp. 262-277
    • Radon, J.1
  • 176
    • 0027211908 scopus 로고
    • Kinesin follows the microtubule's protofilament axis
    • Ray S., Meyhofer E., Milligan R.A., Howard J. Kinesin follows the microtubule's protofilament axis. J. Cell Biol. 1993, 121:1083-1093.
    • (1993) J. Cell Biol. , vol.121 , pp. 1083-1093
    • Ray, S.1    Meyhofer, E.2    Milligan, R.A.3    Howard, J.4
  • 177
    • 0001195918 scopus 로고
    • On the theory of optical images, with special reference to the microscope
    • Rayleigh Lord On the theory of optical images, with special reference to the microscope. Phil. Mag. 1896, 42:167-195.
    • (1896) Phil. Mag. , vol.42 , pp. 167-195
    • Rayleigh, L.1
  • 180
    • 0040138365 scopus 로고
    • Interpretation of Patterson diagrams
    • Robertson J.M. Interpretation of Patterson diagrams. Nature 1943, 152:411.
    • (1943) Nature , vol.152 , pp. 411
    • Robertson, J.M.1
  • 181
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 2003, 333:721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 182
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann M.G., Blow D.M. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr. 1962, 15:24-31.
    • (1962) Acta Crystallogr. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 183
    • 0002008141 scopus 로고
    • Determination of phases by the conditions of non-crystallographic symmetry
    • Rossmann M.G., Blow D.M. Determination of phases by the conditions of non-crystallographic symmetry. Acta Crystallogr. 1963, 16:39-45.
    • (1963) Acta Crystallogr. , vol.16 , pp. 39-45
    • Rossmann, M.G.1    Blow, D.M.2
  • 185
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus
    • Sachse C., Chen J.Z., Coureux P.-D., Stroupe M.E., Fändrich M., Grigorieff N. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J. Mol. Biol. 2007, 371:812-835.
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.Z.2    Coureux, P.-D.3    Stroupe, M.E.4    Fändrich, M.5    Grigorieff, N.6
  • 186
    • 0017477892 scopus 로고
    • Motif detection in quantum noise-limited electron micrographs by cross-correlation
    • Saxton W.O., Frank J. Motif detection in quantum noise-limited electron micrographs by cross-correlation. Ultramicroscopy 1977, 2:219-227.
    • (1977) Ultramicroscopy , vol.2 , pp. 219-227
    • Saxton, W.O.1    Frank, J.2
  • 187
    • 0019987933 scopus 로고
    • The correlation averaging of regularly arranged bacterial cell envelope protein
    • Saxton W.O., Baumeister W. The correlation averaging of regularly arranged bacterial cell envelope protein. J. Microsc. 1982, 127:127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 188
    • 0025395829 scopus 로고
    • Invariant classification of molecular views in electron micrographs
    • Schatz M., van Heel M. Invariant classification of molecular views in electron micrographs. Ultramicroscopy 1990, 32:255-264.
    • (1990) Ultramicroscopy , vol.32 , pp. 255-264
    • Schatz, M.1    van Heel, M.2
  • 189
    • 0242278253 scopus 로고
    • U die;ber einige Fehler von Elektronenlinsen
    • Scherzer O. Über einige Fehler von Elektronenlinsen. Z. Physik. 1936, 101:593-603.
    • (1936) Z. Physik. , vol.101 , pp. 593-603
    • Scherzer, O.1
  • 190
    • 0002170585 scopus 로고
    • The theoretical resolution limit of the electron microscope
    • Scherzer O. The theoretical resolution limit of the electron microscope. J. Appl. Phys. 1949, 20:20-29.
    • (1949) J. Appl. Phys. , vol.20 , pp. 20-29
    • Scherzer, O.1
  • 191
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing T.M., Ramakrishnan V. What recent ribosome structures have revealed about the mechanism of translation. Nature 2009, 461:1234-1242.
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 192
  • 193
    • 67349183743 scopus 로고    scopus 로고
    • Structure of hepatitis B surface antigen from subviral tubes determined by electron cryomicroscopy
    • Short J.M., Chen S., Roseman A.M., Butler P.J.G., Crowther R.A. Structure of hepatitis B surface antigen from subviral tubes determined by electron cryomicroscopy. J. Mol. Biol. 2009, 390:135-141.
    • (2009) J. Mol. Biol. , vol.390 , pp. 135-141
    • Short, J.M.1    Chen, S.2    Roseman, A.M.3    Butler, P.J.G.4    Crowther, R.A.5
  • 194
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • Schröder G.F., Levitt M., Brunger A.T. Super-resolution biomolecular crystallography with low-resolution data. Nature 2010, 464:1218-1222.
    • (2010) Nature , vol.464 , pp. 1218-1222
    • Schröder, G.F.1    Levitt, M.2    Brunger, A.T.3
  • 196
    • 0026663109 scopus 로고
    • Quantitation of molecular densities by cryo-electron microscopy. Determination of the radial density distribution of tobacco mosaic virus
    • Smith M.F., Langmore J.P. Quantitation of molecular densities by cryo-electron microscopy. Determination of the radial density distribution of tobacco mosaic virus. J. Mol. Biol. 1992, 226:763-774.
    • (1992) J. Mol. Biol. , vol.226 , pp. 763-774
    • Smith, M.F.1    Langmore, J.P.2
  • 200
    • 0001420610 scopus 로고
    • Computer image processing of electron micrographs of biological structures with helical symmetry
    • Stewart M. Computer image processing of electron micrographs of biological structures with helical symmetry. J. Electron Microsc. Tech. 1988, 9:325-358.
    • (1988) J. Electron Microsc. Tech. , vol.9 , pp. 325-358
    • Stewart, M.1
  • 201
    • 0014322650 scopus 로고
    • Further characterization of particulate fractions from lysed cell envelopes of Halobacter halobium and isolation of gas vacuole membranes
    • Stoeckenius W., Kunau W.H. Further characterization of particulate fractions from lysed cell envelopes of Halobacter halobium and isolation of gas vacuole membranes. J. Cell Biol. 1968, 38:337-357.
    • (1968) J. Cell Biol. , vol.38 , pp. 337-357
    • Stoeckenius, W.1    Kunau, W.H.2
  • 202
    • 80053050698 scopus 로고
    • Optical methods in X-ray analysis. I. The study of imperfect structures
    • Taylor C.A., Hinde R.M., Lipson H. Optical methods in X-ray analysis. I. The study of imperfect structures. Acta Crystallogr. 1951, 4:261.
    • (1951) Acta Crystallogr. , vol.4 , pp. 261
    • Taylor, C.A.1    Hinde, R.M.2    Lipson, H.3
  • 204
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor K.A., Glaeser R.M. Electron diffraction of frozen, hydrated protein crystals. Science 1974, 186:1036-1037.
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 205
    • 0017140343 scopus 로고
    • Electron microscopy of frozen hydrated biological specimens
    • Taylor K.A., Glaeser R.M. Electron microscopy of frozen hydrated biological specimens. J. Ultrastruct. Res. 1976, 55:448-456.
    • (1976) J. Ultrastruct. Res. , vol.55 , pp. 448-456
    • Taylor, K.A.1    Glaeser, R.M.2
  • 206
    • 84944439230 scopus 로고
    • Zur Defokussierungsabha die;ngigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung
    • Thon F. Zur Defokussierungsabhängigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung. Z. Naturforschg 1966, 21a:476-478.
    • (1966) Z. Naturforschg , vol.21 a , pp. 476-478
    • Thon, F.1
  • 208
    • 0030739033 scopus 로고    scopus 로고
    • Bivalent binding of a neutralizing antibody to a calcivirus involves the torsional flexibility of the antibody hinge
    • Thouvenin E., Laurent S., Madelaine M.-F., Rasschaert D., Vautherot J.-F., Hewat E.A. Bivalent binding of a neutralizing antibody to a calcivirus involves the torsional flexibility of the antibody hinge. J. Mol. Biol. 1997, 270:238-246.
    • (1997) J. Mol. Biol. , vol.270 , pp. 238-246
    • Thouvenin, E.1    Laurent, S.2    Madelaine, M.-F.3    Rasschaert, D.4    Vautherot, J.-F.5    Hewat, E.A.6
  • 209
    • 0034044540 scopus 로고    scopus 로고
    • Reconstruction principles of icosahedral virus structure determination using electron cryomicroscopy
    • Thuman-Commike P.A., Chiu W. Reconstruction principles of icosahedral virus structure determination using electron cryomicroscopy. Micron. 2000, 31(6):687-711.
    • (2000) Micron. , vol.31 , Issue.6 , pp. 687-711
    • Thuman-Commike, P.A.1    Chiu, W.2
  • 210
    • 0023820449 scopus 로고
    • Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images
    • Toyoshima C., Unwin N. Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images. Ultramicroscopy 1988, 25:279-292.
    • (1988) Ultramicroscopy , vol.25 , pp. 279-292
    • Toyoshima, C.1    Unwin, N.2
  • 211
    • 0034034591 scopus 로고    scopus 로고
    • Structure determination of tubular crystals of membrane proteins. 1. Indexing of diffraction patterns
    • Toyoshima C. Structure determination of tubular crystals of membrane proteins. 1. Indexing of diffraction patterns. Ultramicroscopy 2000, 84:1-14.
    • (2000) Ultramicroscopy , vol.84 , pp. 1-14
    • Toyoshima, C.1
  • 212
    • 0032489409 scopus 로고    scopus 로고
    • Non-helical perturbations of the flagellar filament: Salmonella typhimurium SJW117 at 9.6 A ring; resolution
    • Trachtenberg S., DeRosier D.J., Zemlin F., Beckmann Non-helical perturbations of the flagellar filament: Salmonella typhimurium SJW117 at 9.6 Å resolution. J. Mol. Biol. 1998, 276:759-773.
    • (1998) J. Mol. Biol. , vol.276 , pp. 759-773
    • Trachtenberg, S.1    DeRosier, D.J.2    Zemlin, F.3    Beckmann4
  • 213
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P.N.T., Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 1975, 94:425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 214
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 A ring; resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 2005, 346:967-989.
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 215
    • 0028059991 scopus 로고
    • Analysis of electron microscope images and electron diffraction patterns of thin crystals of Phi;29 connectors in ice
    • Valpuesta J.-M., Carrascosa J.L., Henderson R. Analysis of electron microscope images and electron diffraction patterns of thin crystals of Φ29 connectors in ice. J. Mol. Biol. 1994, 240:281-287.
    • (1994) J. Mol. Biol. , vol.240 , pp. 281-287
    • Valpuesta, J.-M.1    Carrascosa, J.L.2    Henderson, R.3
  • 217
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel M. Similarity measures between images. Ultramicroscopy 1987, 21:95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • van Heel, M.1
  • 219
    • 84875242004 scopus 로고    scopus 로고
    • Multivariate statistical analysis in single particle (cryo) electron microscopy
    • 3D-EM in Life Sciences (Sixth Framework Paper). (DVD).
    • van Heel, M., Portugal, R., Schatz, M., 2009. Multivariate statistical analysis in single particle (cryo) electron microscopy. 3D-EM in Life Sciences (Sixth Framework Paper). (DVD). http://www.single_particles.org.
    • (2009)
    • van Heel, M.1    Portugal, R.2    Schatz, M.3
  • 220
    • 20444440419 scopus 로고    scopus 로고
    • Normal mode calculations of icosahedral viruses with full dihedral flexibility by use of molecular symmetry
    • van Vlijmen H.W.T., Karplus M. Normal mode calculations of icosahedral viruses with full dihedral flexibility by use of molecular symmetry. J. Mol. Biol. 2005, 350:528-542.
    • (2005) J. Mol. Biol. , vol.350 , pp. 528-542
    • van Vlijmen, H.W.T.1    Karplus, M.2
  • 224
    • 84944178665 scopus 로고
    • Hierarchical grouping to optimize an objective function
    • Ward J.H. Hierarchical grouping to optimize an objective function. Am. Statist. Assoc. J. 1963, 58:236-244.
    • (1963) Am. Statist. Assoc. J. , vol.58 , pp. 236-244
    • Ward, J.H.1
  • 225
    • 0006792785 scopus 로고
    • Fourier transforms and scattering of tubular objects
    • Waser J. Fourier transforms and scattering of tubular objects. Acta. Crystallogr. 1955, 8:142-150.
    • (1955) Acta. Crystallogr. , vol.8 , pp. 142-150
    • Waser, J.1
  • 227
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids. A structure for deoxyribose nucleic acid
    • Watson J.D., Crick F.H.C. Molecular structure of nucleic acids. A structure for deoxyribose nucleic acid. Nature 1953, 171:737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 228
    • 0004158366 scopus 로고
    • University Press, Princeton
    • Weyl H. Symmetry 1952, University Press, Princeton.
    • (1952) Symmetry
    • Weyl, H.1
  • 229
    • 0742272143 scopus 로고    scopus 로고
    • Recognition and separation of single particles with size variation by statistical analysis of their images
    • White H.E., Saibil H.R., Ignatiou A., Orlova E.V. Recognition and separation of single particles with size variation by statistical analysis of their images. J. Mol. Biol. 2004, 336:453-480.
    • (2004) J. Mol. Biol. , vol.336 , pp. 453-480
    • White, H.E.1    Saibil, H.R.2    Ignatiou, A.3    Orlova, E.V.4
  • 230
    • 0001693842 scopus 로고
    • On the functions which are represented by the expansions of the interpolatory theory
    • Whittaker E.T. On the functions which are represented by the expansions of the interpolatory theory. Proc. Roy. Soc. Edinburgh 1915, 35:181-194.
    • (1915) Proc. Roy. Soc. Edinburgh , vol.35 , pp. 181-194
    • Whittaker, E.T.1
  • 231
    • 0014426672 scopus 로고
    • Crystallographic determination of symmetry of aspartate transcarbamylase: studies of trigonal and tetragonal crystalline forms of aspartate transcarbamylase show that the molecule has a three-fold and a two-fold symmetry axis
    • Wiley D.C., Lipscomb W.N. Crystallographic determination of symmetry of aspartate transcarbamylase: studies of trigonal and tetragonal crystalline forms of aspartate transcarbamylase show that the molecule has a three-fold and a two-fold symmetry axis. Nature 1968, 218:1119-1121.
    • (1968) Nature , vol.218 , pp. 1119-1121
    • Wiley, D.C.1    Lipscomb, W.N.2
  • 232
    • 0014966182 scopus 로고
    • Electron microscopy of tobacco mosaic virus under conditions of minimal beam exposure
    • Williams R.C., Fisher H.W. Electron microscopy of tobacco mosaic virus under conditions of minimal beam exposure. J. Mol. Biol. 1970, 52:121-123.
    • (1970) J. Mol. Biol. , vol.52 , pp. 121-123
    • Williams, R.C.1    Fisher, H.W.2
  • 233
    • 0000984347 scopus 로고
    • Determination of absolute from relative X-ray intensity data
    • Wilson A.J.C. Determination of absolute from relative X-ray intensity data. Nature 1942, 150:152.
    • (1942) Nature , vol.150 , pp. 152
    • Wilson, A.J.C.1
  • 236
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne S.A., Crowther R.A., Leslie A.G. The crystal structure of the human hepatitis B virus capsid. Mol. Cell. 1999, 3:771-780.
    • (1999) Mol. Cell. , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 237
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 2003, 424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 238
    • 0036805571 scopus 로고    scopus 로고
    • Diffractogram tableaux by mouse click
    • Zemlin J., Zemlin F. Diffractogram tableaux by mouse click. Ultramicroscopy 2002, 93:77-82.
    • (2002) Ultramicroscopy , vol.93 , pp. 77-82
    • Zemlin, J.1    Zemlin, F.2
  • 239
    • 84897993817 scopus 로고    scopus 로고
    • 3.3 A ring; cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X., Fang Q., Hui W.H., Zhou Z.H. 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 2010, 141:1-11.
    • (2010) Cell , vol.141 , pp. 1-11
    • Zhang, X.1    Fang, Q.2    Hui, W.H.3    Zhou, Z.H.4
  • 240
    • 0042827239 scopus 로고    scopus 로고
    • Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution
    • Zhou Z.H., Chiu W. Determination of icosahedral virus structures by electron cryomicroscopy at subnanometer resolution. Adv. Protein Chem. 2002, 64:93-124.
    • (2002) Adv. Protein Chem. , vol.64 , pp. 93-124
    • Zhou, Z.H.1    Chiu, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.