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Volumn 28, Issue 2, 1995, Pages 171-193

The Potential and Limitations of Neutrons, Electrons and X-Rays for Atomic Resolution Microscopy of Unstained Biological Molecules

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[No Author keywords available]

Indexed keywords

NITROGEN 15;

EID: 0029003107     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S003358350000305X     Document Type: Article
Times cited : (932)

References (42)
  • 1
    • 70349858779 scopus 로고
    • Handbook of Mathematical Functions with Formulas, Graphs and Mathematical Tables
    • ABRAMOWITZ, M. & STEGUN, I. A. (1965). Handbook of Mathematical Functions with Formulas, Graphs and Mathematical Tables. New York: Dover Publications.
    • (1965) New York: Dover Publications
    • ABRAMOWITZ, M.1    STEGUN, I.A.2
  • 3
    • 0021404749 scopus 로고
    • Optimum X-ray wavelength for protein crystallography
    • ARNDT, U. (1984). Optimum X-ray wavelength for protein crystallography. J. Appl. Cryst. 17, 118–119.
    • (1984) J. Appl. Cryst. , vol.17 , pp. 118-119
    • ARNDT, U.1
  • 4
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses - analysis by cryoelectron microscopy and 3-dimensional image-reconstruction
    • BAKER, T. S., NEWCOMB, W. W., OLSON, N. H., COWSERT, L. M., OLSON, C. & BROWN, J. D. C. (1991). Structures of bovine and human papillomaviruses - analysis by cryoelectron microscopy and 3-dimensional image-reconstruction. Biophys. J. 60, 1445–1456.
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • BAKER, T.S.1    NEWCOMB, W.W.2    OLSON, N.H.3    COWSERT, L.M.4    OLSON, C.5    BROWN, J.D.C.6
  • 5
    • 0040310859 scopus 로고
    • Molecular microscopy: fundamental limitations
    • BREEDLOVE, J. R. & TRAMMELL, G. T. (1970). Molecular microscopy: fundamental limitations. Science, 170, 1310–1313.
    • (1970) Science , vol.170 , pp. 1310-1313
    • BREEDLOVE, J.R.1    TRAMMELL, G.T.2
  • 6
    • 84976081654 scopus 로고
    • Diffraction Physics Amsterdam: North-Holland
    • COWLEY, J. M. (1975). Diffraction Physics Amsterdam: North-Holland.
    • (1975)
    • COWLEY, J.M.1
  • 7
    • 0000505808 scopus 로고
    • The theory of X-ray reflexion
    • DARWIN, C. G. (1914). The theory of X-ray reflexion. Phil. Mag. 27, 315–333.
    • (1914) Phil. Mag. , vol.27 , pp. 315-333
    • DARWIN, C.G.1
  • 8
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DE ROSIER, D. J. & KLUG, A. (1968). Reconstruction of three-dimensional structures from electron micrographs. Nature 217, 130–134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DE ROSIER, D.J.1    KLUG, A.2
  • 9
    • 0000186608 scopus 로고
    • Measurement and compensation of defocusing and aberrations by Fourier processing of electron micrographs
    • ERICKSON, H. & KLUG, A. (1971). Measurement and compensation of defocusing and aberrations by Fourier processing of electron micrographs. Phil. Trans. Roy. Soc. Lond., B 261, 105–118.
    • (1971) Phil. Trans. Roy. Soc. Lond. , vol.261 , pp. 105-118
    • ERICKSON, H.1    KLUG, A.2
  • 10
    • 34250769340 scopus 로고
    • A new microscopic principle
    • GABOR, D. (1948). A new microscopic principle. Nature, 161, 777–778.
    • (1948) Nature , vol.161 , pp. 777-778
    • GABOR, D.1
  • 11
    • 0000520380 scopus 로고
    • High-voltage electron diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical
    • GLAESER, R. M. & CESKA, T. A. (1989). High-voltage electron diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical. Acta Cryst. A45, 620–628.
    • (1989) Acta Cryst , vol.A45 , pp. 620-628
    • GLAESER, R.M.1    CESKA, T.A.2
  • 12
    • 0000058559 scopus 로고
    • Cryo-protection of protein crystals in intense X-ray beams
    • GONZALEZ, A., THOMPSON, A. W. & NAVE, C. (1992). Cryo-protection of protein crystals in intense X-ray beams. Rev. Sci. Instrum. 63, 1177–1180.
    • (1992) Rev. Sci. Instrum. , vol.63 , pp. 1177-1180
    • GONZALEZ, A.1    THOMPSON, A.W.2    NAVE, C.3
  • 13
    • 0025071357 scopus 로고
    • Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction
    • HENDERSON, R. (1990). Cryo-protection of protein crystals against radiation damage in electron and X-ray diffraction. Proc. Roy. Soc. B 241, 6–8.
    • (1990) Proc. Roy. Soc. , vol.241 , pp. 6-8
    • HENDERSON, R.1
  • 14
    • 0026523919 scopus 로고
    • Image contrast in high resolution electron microscopy of biological macromolecules: TMC in ice
    • HENDERSON, R. (1992). Image contrast in high resolution electron microscopy of biological macromolecules: TMC in ice. Ultramicroscopy 46, 1–18.
    • (1992) Ultramicroscopy , vol.46 , pp. 1-18
    • HENDERSON, R.1
  • 15
    • 0021786909 scopus 로고
    • Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals
    • HENDERSON, R. & GLAESER, R. M. (1985). Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals. Ultramicroscopy 16, 139–150.
    • (1985) Ultramicroscopy , vol.16 , pp. 139-150
    • HENDERSON, R.1    GLAESER, R.M.2
  • 16
    • 0025292355 scopus 로고
    • A model for the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy
    • HENDERSON, R., BALDWIN, J. M., CESKA, T. A., BECKMANN, E., ZEMLIN, F. & DOWNING, K. (1990). A model for the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy. J. Mol. Biol. 213, 899–929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • HENDERSON, R.1    BALDWIN, J.M.2    CESKA, T.A.3    BECKMANN, E.4    ZEMLIN, F.5    DOWNING, K.6
  • 17
    • 0040808579 scopus 로고
    • Electron diffraction with the transmission electron microscope as a phase-determining diffractometer - from spatial frequency filtering to the three-dimensional structure analysis of ribosomes
    • HOPPE, W. (1983). Electron diffraction with the transmission electron microscope as a phase-determining diffractometer - from spatial frequency filtering to the three-dimensional structure analysis of ribosomes. Angew. Chem. Int. Ed. Engl. 22, 456–485.
    • (1983) Angew. Chem. Int. Ed. Engl. , vol.22 , pp. 456-485
    • HOPPE, W.1
  • 18
    • 84886755383 scopus 로고
    • Pair, triplet and total atomic cross sections (and mass attenuation coefficients) for 1Mev-100Gev photons in elements Z = 1 to 100
    • HUBBELL, J. H., GIMM, H. A. & OVERBO, I. (1980). Pair, triplet and total atomic cross sections (and mass attenuation coefficients) for 1Mev-100Gev photons in elements Z = 1 to 100. J. Phys. Chem. Ref. Data 9, 1023–1147.
    • (1980) J. Phys. Chem. Ref. Data , vol.9 , pp. 1023-1147
    • HUBBELL, J.H.1    GIMM, H.A.2    OVERBO, I.3
  • 20
    • 0025806797 scopus 로고
    • Structural architecture of an outer-membrane channel as determined by electron crystallography
    • JAP, B. K., WALIAN, P. J. & GEHRING, K. (1991). Structural architecture of an outer-membrane channel as determined by electron crystallography. Nature 350, 167–170.
    • (1991) Nature , vol.350 , pp. 167-170
    • JAP, B.K.1    WALIAN, P.J.2    GEHRING, K.3
  • 21
    • 0024961660 scopus 로고
    • Visualisation of alpha-helices in tobacco mosaic virus by cryo-electron microscopy
    • JENG, T.-W., CROWTHER, R. A., STUBBS, G. & CHIU, W. (1989). Visualisation of alpha-helices in tobacco mosaic virus by cryo-electron microscopy. J. Mol. Biol. 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
  • 23
    • 0025898707 scopus 로고
    • Three-dimensional structure of plant light-harvesting complex determined by electron crystallography
    • KUHLBRANDT, W. & WANG, D. N. (1991). Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 350, 130–134.
    • (1991) Nature , vol.350 , pp. 130-134
    • KUHLBRANDT, W.1    WANG, D.N.2
  • 24
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • KUHLBRANDT, W., WANG, D. N. & FUJIYOSHI, Y. (1994). Atomic model of plant light-harvesting complex by electron crystallography. Nature 367,.614–621
    • (1994) Nature , vol.367 , pp. 614-621
    • KUHLBRANDT, W.1    WANG, D.N.2    FUJIYOSHI, Y.3
  • 25
    • 0026499195 scopus 로고
    • Quantitative energy-filtered electron microscopy of biological molecules in ice
    • LANGMORE, J. P. & SMITH, M. F. (1992). Quantitative energy-filtered electron microscopy of biological molecules in ice. Ultramicroscopy 46, 349—373.
    • (1992) Ultramicroscopy , vol.46 , pp. 349-373
    • LANGMORE, J.P.1    SMITH, M.F.2
  • 26
    • 0026244960 scopus 로고
    • Optimum focus for taking electron holograms
    • LICHT, H. (1991). Optimum focus for taking electron holograms. Ultramicroscopy 38, 13–22.
    • (1991) Ultramicroscopy , vol.38 , pp. 13-22
    • LICHT, H.1
  • 27
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • PENCZEK, P., RADERMACHER, M. & FRANK, J. (1992). Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 40, 33–53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • PENCZEK, P.1    RADERMACHER, M.2    FRANK, J.3
  • 28
    • 0003521686 scopus 로고
    • Transmission Electron Microscopy
    • 2nd ed. Berlin: Springer-Verlag
    • REIMER, L. (1989). Transmission Electron Microscopy, 2nd ed. Berlin: Springer-Verlag.
    • (1989)
    • REIMER, L.1
  • 29
    • 84976001636 scopus 로고
    • X-ray microscopy
    • (In press)
    • SAYRE, D. & CHAPMAN, H. N. (1994). X-ray microscopy. Acta Cryst. A 51 (In press).
    • (1994) Acta Cryst , vol.51
    • SAYRE, D.1    CHAPMAN, H.N.2
  • 30
    • 0017622664 scopus 로고
    • Transmission microscopy of unmodified biological materials: comparative radiation dosages with electrons and ultrasoft X-ray photons
    • SAYRE, D., KIRZ, J., FEDER, R., KIM, D. M. & SPILLER, E. (1977). Transmission microscopy of unmodified biological materials: comparative radiation dosages with electrons and ultrasoft X-ray photons. Ultramicroscopy 2, 337–349.
    • (1977) Ultramicroscopy , vol.2 , pp. 337-349
    • SAYRE, D.1    KIRZ, J.2    FEDER, R.3    KIM, D.M.4    SPILLER, E.5
  • 31
    • 84915486634 scopus 로고
    • Neutron scattering lengths and cross-sections
    • SEARS, V. F. (1992). Neutron scattering lengths and cross-sections.Neutron News 3(3), 26–37.
    • (1992) Neutron News , vol.3 , Issue.3 , pp. 26-37
    • SEARS, V.F.1
  • 32
    • 0026663109 scopus 로고
    • Quantitation of molecular densities in cryo-electron microscopy: determination of the radial density distribution of tobacco mosaic virus
    • SMITH, M. F. & LANGMORE, J. P. (1992). Quantitation of molecular densities in cryo-electron microscopy: determination of the radial density distribution of tobacco mosaic virus. J. Mol. Biol. 226, 763–774.
    • (1992) J. Mol. Biol. , vol.226 , pp. 763-774
    • SMITH, M.F.1    LANGMORE, J.P.2
  • 33
    • 0003693963 scopus 로고
    • Experimental High-Resolution Electron Microscopy
    • 2nd ed., Oxford University Press
    • SPENCE, J. C. H. (1988). Experimental High-Resolution Electron Microscopy, 2nd ed., Oxford University Press.
    • (1988)
    • SPENCE, J.C.H.1
  • 34
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organisation of Adenovirus
    • Cell
    • STEWART, P. L., BURNETT, R. M., CYRKLAFF, M. & FULLER, S. D. (1991). Image reconstruction reveals the complex molecular organisation of Adenovirus. Cell 67, 145 - 154.
    • (1991) , vol.67 , pp. 145-154
    • STEWART, P.L.1    BURNETT, R.M.2    CYRKLAFF, M.3    FULLER, S.D.4
  • 35
    • 0024301787 scopus 로고
    • Ultracold neutrons: production and experiments
    • STEYERL, A. (1989). Ultracold neutrons: production and experiments. Physica B, 156, 528–533.
    • (1989) Physica B , vol.156 , pp. 528-533
    • STEYERL, A.1
  • 37
    • 84944439230 scopus 로고
    • Zur Defokussierungsabhangigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung
    • THON, F. (1966). Zur Defokussierungsabhangigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung. Z. Naturforsh. 219, 476–478.
    • (1966) Z. Naturforsh , vol.219 , pp. 476-478
    • THON, F.1
  • 38
    • 0002387674 scopus 로고
    • Electron-holographic interference microscopy
    • TONOMURA, A. (1992). Electron-holographic interference microscopy. Adv. Physics 41, 59–103.
    • (1992) Adv. Physics , vol.41 , pp. 59-103
    • TONOMURA, A.1
  • 39
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • TOYOSHIMA, C., SASABE, H. & STOKES, D. L. (1993). Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature 362, 469 – 471.
    • (1993) Nature , vol.362 , pp. 469-471
    • TOYOSHIMA, C.1    SASABE, H.2    STOKES, D.L.3
  • 40
    • 0023820449 scopus 로고
    • Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images
    • TOYOSHIMA, C. & UNWIN, N. (1988a). Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images. Ultramicroscopy 25, 279–292.
    • (1988) Ultramicroscopy , vol.25 , pp. 279-292
    • TOYOSHIMA, C.1    UNWIN, N.2
  • 41
    • 0024290709 scopus 로고
    • Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membrane
    • TOYOSHIMA, C. & UNWIN, N. (1988). Ion channel of acetylcholine receptor reconstructed from images of postsynaptic membrane. Nature 336, 247–250.
    • (1988) Nature , vol.336 , pp. 247-250
    • TOYOSHIMA, C.1    UNWIN, N.2
  • 42
    • 0000210496 scopus 로고
    • How I discovered phase contrast
    • ZERNIKE, F. (1955). How I discovered phase contrast. Science 121, 345–349.
    • (1955) Science , vol.121 , pp. 345-349
    • ZERNIKE, F.1


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