메뉴 건너뛰기




Volumn 163, Issue 3, 2008, Pages 271-276

Retrospective: Radiation damage and its associated "Information Limitations"

Author keywords

Beam induced movement; Biological specimens; Electron microscopy; Radiation damage

Indexed keywords

HELIUM; NITROGEN;

EID: 51349143018     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.06.001     Document Type: Article
Times cited : (70)

References (48)
  • 2
    • 0025970346 scopus 로고
    • Contrast analysis of cryo-images of n-paraffin recorded at 400 kV out to 2.1 Ångstrom resolution
    • Brink J., and Chiu W. Contrast analysis of cryo-images of n-paraffin recorded at 400 kV out to 2.1 Ångstrom resolution. Journal of Microscopy 161 (1991) 279-295
    • (1991) Journal of Microscopy , vol.161 , pp. 279-295
    • Brink, J.1    Chiu, W.2
  • 5
    • 28944435740 scopus 로고    scopus 로고
    • Dose tolerance at helium and nitrogen temperatures for whole cell electron tomography
    • Comolli L.R., and Downing K.H. Dose tolerance at helium and nitrogen temperatures for whole cell electron tomography. Journal of Structural Biology 152 (2005) 149-156
    • (2005) Journal of Structural Biology , vol.152 , pp. 149-156
    • Comolli, L.R.1    Downing, K.H.2
  • 8
    • 0015106320 scopus 로고
    • Limitations to significant information in biological electron microscopy as a result of radiation damage
    • Glaeser R.M. Limitations to significant information in biological electron microscopy as a result of radiation damage. Journal of Ultrastructure Research 36 (1971) 466-482
    • (1971) Journal of Ultrastructure Research , vol.36 , pp. 466-482
    • Glaeser, R.M.1
  • 9
    • 0033377941 scopus 로고    scopus 로고
    • Review: electron crystallography: present excitement, a nod to the past, anticipating the future
    • Glaeser R.M. Review: electron crystallography: present excitement, a nod to the past, anticipating the future. Journal of Structural Biology 128 (1999) 3-14
    • (1999) Journal of Structural Biology , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 10
    • 1442263375 scopus 로고    scopus 로고
    • Specimen charging on thin films with one conducting layer: discussion of physical principles
    • Glaeser R.M., and Downing K.H. Specimen charging on thin films with one conducting layer: discussion of physical principles. Microscopy and Microanalysis 10 (2004) 790-796
    • (2004) Microscopy and Microanalysis , vol.10 , pp. 790-796
    • Glaeser, R.M.1    Downing, K.H.2
  • 12
    • 0016703615 scopus 로고
    • Radiation damage in stained catalase at low temperature
    • Glaeser R.M., and Hobbs L.W. Radiation damage in stained catalase at low temperature. Journal of Microscopy 103 (1975) 209-214
    • (1975) Journal of Microscopy , vol.103 , pp. 209-214
    • Glaeser, R.M.1    Hobbs, L.W.2
  • 13
    • 51349162330 scopus 로고    scopus 로고
    • Glaeser, R.M., Kuo, I., Budinger, T.F., 1971. Method for processing of periodic images at reduced levels of electron irradiation. Proceedings Electron Microscopy Society of America (Boston).
    • Glaeser, R.M., Kuo, I., Budinger, T.F., 1971. Method for processing of periodic images at reduced levels of electron irradiation. Proceedings Electron Microscopy Society of America (Boston).
  • 14
    • 0017873876 scopus 로고
    • Radiation damage relative to transmission electron microscopy of biological specimens at low temperature-review
    • Glaeser R.M., and Taylor K.A. Radiation damage relative to transmission electron microscopy of biological specimens at low temperature-review. Journal of Microscopy 112 (1978) 127-138
    • (1978) Journal of Microscopy , vol.112 , pp. 127-138
    • Glaeser, R.M.1    Taylor, K.A.2
  • 15
    • 0014578252 scopus 로고
    • Application of electron diffraction to biological electron microscopy
    • Glaeser R.M., and Thomas G. Application of electron diffraction to biological electron microscopy. Biophysical Journal 9 (1969) 1073-1099
    • (1969) Biophysical Journal , vol.9 , pp. 1073-1099
    • Glaeser, R.M.1    Thomas, G.2
  • 17
    • 0029620939 scopus 로고
    • Lipid location in deoxycholate-treated purple membrane at 2.6 Ångstrom
    • Grigorieff N., Beckmann E., and Zemlin F. Lipid location in deoxycholate-treated purple membrane at 2.6 Ångstrom. Journal of Molecular Biology 254 (1995) 404-415
    • (1995) Journal of Molecular Biology , vol.254 , pp. 404-415
    • Grigorieff, N.1    Beckmann, E.2    Zemlin, F.3
  • 18
    • 0018333925 scopus 로고
    • Radiation damage of purple membrane at low temperature
    • Hayward S.B., and Glaeser R.M. Radiation damage of purple membrane at low temperature. Ultramicroscopy 4 (1979) 201-210
    • (1979) Ultramicroscopy , vol.4 , pp. 201-210
    • Hayward, S.B.1    Glaeser, R.M.2
  • 19
    • 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. Quarterly Reviews of Biophysics 28 (1995) 171-193
    • (1995) Quarterly Reviews of Biophysics , vol.28 , pp. 171-193
    • Henderson, R.1
  • 20
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium-recording, measurement and evaluation of electron micrographs at 3.5 Ångstrom resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., and Zemlin F. Structure of purple membrane from Halobacterium halobium-recording, measurement and evaluation of electron micrographs at 3.5 Ångstrom resolution. Ultramicroscopy 19 (1986) 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
  • 21
    • 0021786909 scopus 로고
    • Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals
    • Henderson R., and Glaeser R.M. Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals. Ultramicroscopy 16 (1985) 139-150
    • (1985) Ultramicroscopy , vol.16 , pp. 139-150
    • Henderson, R.1    Glaeser, R.M.2
  • 22
    • 0345305377 scopus 로고    scopus 로고
    • Diffraction imaging of single particles and biomolecules
    • Huldt G., Szoke A., and Hajdu J. Diffraction imaging of single particles and biomolecules. Journal of Structural Biology 144 (2003) 219-227
    • (2003) Journal of Structural Biology , vol.144 , pp. 219-227
    • Huldt, G.1    Szoke, A.2    Hajdu, J.3
  • 23
    • 32544437801 scopus 로고    scopus 로고
    • A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography
    • Iancu C.V., Wright E.R., Heymann J.B., and Jensen G.J. A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography. Journal of Structural Biology 153 (2006) 231-240
    • (2006) Journal of Structural Biology , vol.153 , pp. 231-240
    • Iancu, C.V.1    Wright, E.R.2    Heymann, J.B.3    Jensen, G.J.4
  • 24
    • 0024955278 scopus 로고
    • Evaporated carbon stabilizes thin, frozen-hydrated specimens
    • Jakubowski U., Baumeister W., and Glaeser R.M. Evaporated carbon stabilizes thin, frozen-hydrated specimens. Ultramicroscopy 31 (1989) 351-356
    • (1989) Ultramicroscopy , vol.31 , pp. 351-356
    • Jakubowski, U.1    Baumeister, W.2    Glaeser, R.M.3
  • 25
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W., Baker M.L., Jakana J., Weigele P.R., King J., and Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 451 (2008) 1130-1134
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 26
    • 0000789261 scopus 로고
    • Irradiation changes in organic polymers at various accelerating voltages
    • Kobayashi K., and Sakaoku K. Irradiation changes in organic polymers at various accelerating voltages. Laboratory Investigation 14 (1965) 1097-1114
    • (1965) Laboratory Investigation , vol.14 , pp. 1097-1114
    • Kobayashi, K.1    Sakaoku, K.2
  • 27
    • 0016780259 scopus 로고
    • Development of methodology for low exposure, high-resolution electron-microscopy of biological specimens
    • Kuo I.A.M., and Glaeser R.M. Development of methodology for low exposure, high-resolution electron-microscopy of biological specimens. Ultramicroscopy 1 (1975) 53-66
    • (1975) Ultramicroscopy , vol.1 , pp. 53-66
    • Kuo, I.A.M.1    Glaeser, R.M.2
  • 28
    • 0029123968 scopus 로고
    • Cryoelectron energy-loss spectroscopy-observations on vitrified hydrated specimens and radiation damage
    • Leapman R.D., and Sun S.Q. Cryoelectron energy-loss spectroscopy-observations on vitrified hydrated specimens and radiation damage. Ultramicroscopy 59 (1995) 71-79
    • (1995) Ultramicroscopy , vol.59 , pp. 71-79
    • Leapman, R.D.1    Sun, S.Q.2
  • 30
    • 40049105503 scopus 로고    scopus 로고
    • De novo backbone trace of GroEL from single particle electron cryomicroscopy
    • Ludtke S.J., Baker M.L., Chen D.-H., Song J.-L., Chuang D.T., and Chiu W. De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 16 (2008) 441-448
    • (2008) Structure , vol.16 , pp. 441-448
    • Ludtke, S.J.1    Baker, M.L.2    Chen, D.-H.3    Song, J.-L.4    Chuang, D.T.5    Chiu, W.6
  • 32
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Ångstrom resolution based on electron crystallography: implication of the charge distribution
    • Mitsuoka K., Hirai T., Murata K., Miyazawa A., Kidera A., Kimura Y., and Fujiyoshi Y. The structure of bacteriorhodopsin at 3.0 Ångstrom resolution based on electron crystallography: implication of the charge distribution. Journal of Molecular Biology 286 (1999) 861-882
    • (1999) Journal of Molecular Biology , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 33
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A., Fujiyoshi Y., and Unwin N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 (2003) 949-955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 35
    • 0034680144 scopus 로고    scopus 로고
    • Potential for biomolecular imaging with femtosecond X-ray pulses
    • Neutze R., Wouts R., van der Spoel D., Weckert E., and Hajdu J. Potential for biomolecular imaging with femtosecond X-ray pulses. Nature 406 (2000) 752-757
    • (2000) Nature , vol.406 , pp. 752-757
    • Neutze, R.1    Wouts, R.2    van der Spoel, D.3    Weckert, E.4    Hajdu, J.5
  • 36
    • 0032516190 scopus 로고    scopus 로고
    • Structure of the alpha-beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., and Downing K.H. Structure of the alpha-beta tubulin dimer by electron crystallography. Nature 393 (1998) 191
    • (1998) Nature , vol.393 , pp. 191
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 37
    • 51349153958 scopus 로고
    • Irradiation changes in organic and inorganic objects
    • Reimer L. Irradiation changes in organic and inorganic objects. Laboratory Investigation 14 (1965) 1082-1096
    • (1965) Laboratory Investigation , vol.14 , pp. 1082-1096
    • Reimer, L.1
  • 41
    • 0014836409 scopus 로고
    • A Study of mass loss and product formation after irradiation of some dry amino acids, peptides, polypeptides and proteins with an electron beam of low current density
    • Stenn K.S., and Bahr G.F. A Study of mass loss and product formation after irradiation of some dry amino acids, peptides, polypeptides and proteins with an electron beam of low current density. Journal of Histochemistry and Cytochemistry 18 (1970) 574-580
    • (1970) Journal of Histochemistry and Cytochemistry , vol.18 , pp. 574-580
    • Stenn, K.S.1    Bahr, G.F.2
  • 42
    • 0014803266 scopus 로고
    • Specimen damage caused by beam of transmission electron microscope, a correlative reconsideration
    • Stenn K., and Bahr G.F. Specimen damage caused by beam of transmission electron microscope, a correlative reconsideration. Journal of Ultrastructure Research 31 (1970) 526-550
    • (1970) Journal of Ultrastructure Research , vol.31 , pp. 526-550
    • Stenn, K.1    Bahr, G.F.2
  • 43
    • 51349115007 scopus 로고    scopus 로고
    • Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on challenges for the future
    • Taylor K.A., and Glaeser R.M. Retrospective on the early development of cryoelectron microscopy of macromolecules and a prospective on challenges for the future. Journal of Structural Biology 163 (2008) 214-223
    • (2008) Journal of Structural Biology , vol.163 , pp. 214-223
    • Taylor, K.A.1    Glaeser, R.M.2
  • 44
    • 1442338662 scopus 로고    scopus 로고
    • Electron microscopy of biological macromolecules: bridging the gap between what physics allows and what we currently can get
    • Typke D., Downing K.H., and Glaeser R.M. Electron microscopy of biological macromolecules: bridging the gap between what physics allows and what we currently can get. Microscopy and Microanalysis 10 (2004) 21-27
    • (2004) Microscopy and Microanalysis , vol.10 , pp. 21-27
    • Typke, D.1    Downing, K.H.2    Glaeser, R.M.3
  • 45
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P.N.T., and Henderson R. Molecular structure determination by electron microscopy of unstained crystalline specimens. Journal of Molecular Biology 94 (1975) 425-440
    • (1975) Journal of Molecular Biology , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 47
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., and Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424 (2003) 643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.