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Volumn 29, Issue 2-3, 1998, Pages 145-160

Cryo-negative staining

Author keywords

Contrast; Cryo electron microscopy; Macromolecule; Negative staining; Virus; Vitrification

Indexed keywords

AMMONIUM MOLYBDATE; CATALASE; CHAPERONIN; COLORING AGENT; CYSTEINE PROTEINASE; HEMOCYANIN; KEYHOLE LIMPET HEMOCYANIN; KEYHOLE-LIMPET HEMOCYANIN; MOLYBDENUM; MULTIENZYME COMPLEX; PROTEASOME;

EID: 0032052907     PISSN: 09684328     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-4328(97)00068-1     Document Type: Article
Times cited : (139)

References (40)
  • 2
    • 0029670614 scopus 로고    scopus 로고
    • Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography
    • Avila-Sakar, A. J. and Chiu, W., 1996. Visualization of β-sheets and side-chain clusters in two-dimensional periodic arrays of streptavidin on phospholipid monolayers by electron crystallography. Biophys. J., 70, 57-68.
    • (1996) Biophys. J. , vol.70 , pp. 57-68
    • Avila-Sakar, A.J.1    Chiu, W.2
  • 4
    • 0026499357 scopus 로고
    • Has negative staining a future in biomolecular electron microscopy?
    • Bremner, A., Hann, C., Engel, A., Baumeister, W. and Aebi, U., 1992. Has negative staining a future in biomolecular electron microscopy? Ultramicroscopy, 46, 85-111.
    • (1992) Ultramicroscopy , vol.46 , pp. 85-111
    • Bremner, A.1    Hann, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 5
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner, S. and Horne, R. W., 1959. A negative staining method for high resolution electron microscopy of viruses. Biochim. Biophys. Acta, 34, 60-71.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 60-71
    • Brenner, S.1    Horne, R.W.2
  • 6
    • 0028038385 scopus 로고
    • Particle-surface interaction in thin vitrified films for cryo-electron microscopy
    • Cyrklaff, M., Ros, N., Gross, H. and Dubochet, J., 1994. Particle-surface interaction in thin vitrified films for cryo-electron microscopy. J. Microsc., 175, 135-142.
    • (1994) J. Microsc. , vol.175 , pp. 135-142
    • Cyrklaff, M.1    Ros, N.2    Gross, H.3    Dubochet, J.4
  • 7
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs
    • De Rosier, D. J. and Klug, A., 1968. Reconstruction of three-dimensional images from electron micrographs. Nature, 217, 130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • De Rosier, D.J.1    Klug, A.2
  • 8
    • 0010489246 scopus 로고
    • Electron diffraction from single, fully hydrated, ox-liver catalase microcrystals
    • Dorset, D. L. and Parsons, D. F., 1975. Electron diffraction from single, fully hydrated, ox-liver catalase microcrystals. Acta Cryst. A, 31, 210-215.
    • (1975) Acta Cryst. A , vol.31 , pp. 210-215
    • Dorset, D.L.1    Parsons, D.F.2
  • 12
    • 0019707963 scopus 로고
    • SPIDER - A modular software system for electron image processing
    • Frank, J., Shimkin, B. and Dowse, H., 1981. SPIDER - a modular software system for electron image processing. Ultramicroscopy, 6, 343-358.
    • (1981) Ultramicroscopy , vol.6 , pp. 343-358
    • Frank, J.1    Shimkin, B.2    Dowse, H.3
  • 13
    • 0029975088 scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3-D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M. and Leith, A., 1995. SPIDER and WEB: processing and visualization of images in 3-D electron microscopy and related fields. J. Struct. Biol., 116, 190-199.
    • (1995) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 14
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles - The uncommon line
    • Fuller, S. D., Butcher, S. J., Cheng, R. H. and Baker, T. S., 1996. Three-dimensional reconstruction of icosahedral particles - the uncommon line. J. Struct. Biol., 116, 48-65.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-65
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 15
    • 33845184276 scopus 로고
    • Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly
    • Green, J. L. and Angell, C. A., 1989. Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly. J. Phys. Chem., 93, 2880-2882.
    • (1989) J. Phys. Chem. , vol.93 , pp. 2880-2882
    • Green, J.L.1    Angell, C.A.2
  • 17
    • 0003597312 scopus 로고    scopus 로고
    • Negative staining and cryoelectron microscopy
    • BIOS Scientific Publishers Ltd., Oxford, UK
    • Harris, J. R., 1997. Negative staining and cryoelectron microscopy. In RMS Microscopy Handbook Series, Vol. 25. BIOS Scientific Publishers Ltd., Oxford, UK.
    • (1997) RMS Microscopy Handbook Series , vol.25
    • Harris, J.R.1
  • 18
    • 0027723370 scopus 로고
    • Immunoelectron microscopy of keyhole limpet hemocyanin: A parallel subunit model
    • Harris, J. R., Gebauer, W. and Markl, J., 1993. Immunoelectron microscopy of keyhole limpet hemocyanin: a parallel subunit model. J. Struc. Biol., 111, 96-113.
    • (1993) J. Struc. Biol. , vol.111 , pp. 96-113
    • Harris, J.R.1    Gebauer, W.2    Markl, J.3
  • 19
    • 0029159273 scopus 로고
    • Keyhole limpet hemocyanin (KLH): Negative staining in the presence of trehalose
    • Harris, J. R., Gebauer, W. and Markl, J., 1995a. Keyhole limpet hemocyanin (KLH): negative staining in the presence of trehalose. Micron, 26, 25-33.
    • (1995) Micron , vol.26 , pp. 25-33
    • Harris, J.R.1    Gebauer, W.2    Markl, J.3
  • 20
    • 0001383317 scopus 로고
    • Keyhole limpet hemocyanin (KLH): Purification of intact KLH1 through selective dissociation of KLH2
    • Harris, J. R., Gebauer, W., Söhngen, S. M. and Markl, J., 1995b. Keyhole limpet hemocyanin (KLH): purification of intact KLH1 through selective dissociation of KLH2. Micron, 26, 201-212.
    • (1995) Micron , vol.26 , pp. 201-212
    • Harris, J.R.1    Gebauer, W.2    Söhngen, S.M.3    Markl, J.4
  • 21
    • 0031080603 scopus 로고    scopus 로고
    • Keyhole limpet hemocyanin (KLH), II: Characteristic reassociation properties of purified KLH1 and KLH2
    • Harris, J. R., Gebauer, W., Söhngen, S. M., Nermut, M. V. and Markl, J., 1997. Keyhole limpet hemocyanin (KLH), II: characteristic reassociation properties of purified KLH1 and KLH2. Micron, 28, 43-56.
    • (1997) Micron , vol.28 , pp. 43-56
    • Harris, J.R.1    Gebauer, W.2    Söhngen, S.M.3    Nermut, M.V.4    Markl, J.5
  • 22
    • 0028889613 scopus 로고
    • Human erythrocyte catalase: 2-D crystal nucleation and production of multiple crystal forms
    • Harris, J. R. and Holzenburg, A., 1995. Human erythrocyte catalase: 2-D crystal nucleation and production of multiple crystal forms. J. Struct. Biol., 115, 102-112.
    • (1995) J. Struct. Biol. , vol.115 , pp. 102-112
    • Harris, J.R.1    Holzenburg, A.2
  • 23
    • 0028028685 scopus 로고
    • Negative staining: A brief assessment of current technical benefits, limitations and future possibilities
    • Harris, J. R. and Horne, R. W., 1994. Negative staining: a brief assessment of current technical benefits, limitations and future possibilities. Micron, 25, 5-13.
    • (1994) Micron , vol.25 , pp. 5-13
    • Harris, J.R.1    Horne, R.W.2
  • 24
    • 0028559575 scopus 로고
    • Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex
    • Harris, J. R., Plückthun, A. and Zahn, R., 1994. Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex. J. Struct. Biol., 112, 216-230.
    • (1994) J. Struct. Biol. , vol.112 , pp. 216-230
    • Harris, J.R.1    Plückthun, A.2    Zahn, R.3
  • 25
    • 0028842804 scopus 로고
    • Electron microscopy of the GroEL-GroES filament
    • Harris, J. R., Zahn, R. and Plückthun, A., 1995c. Electron microscopy of the GroEL-GroES filament. J. Struct. Biol., 115, 68-77.
    • (1995) J. Struct. Biol. , vol.115 , pp. 68-77
    • Harris, J.R.1    Zahn, R.2    Plückthun, A.3
  • 26
    • 0030567279 scopus 로고    scopus 로고
    • Orientational and spectroscopic studies of Langmuir Blodgett films of a photodynamic pigment protein, allophycocyanin
    • He, J. A., Jiang, L. J., Jiang, L., Bl, Z. C. and Ll, J. R., 1996. Orientational and spectroscopic studies of Langmuir Blodgett films of a photodynamic pigment protein, allophycocyanin. Langmuir, 12, 1840-1845.
    • (1996) Langmuir , vol.12 , pp. 1840-1845
    • He, J.A.1    Jiang, L.J.2    Jiang, L.3    Bl, Z.C.4    Ll, J.R.5
  • 27
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R., 1995. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Quart. Rev. Biophys., 28, 171-193.
    • (1995) Quart. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 28
    • 0030249624 scopus 로고    scopus 로고
    • 3-D reconstructions from ice-embedded and negatively stained biomacromolecular assemblies: A critical comparison
    • Hoenger, A. and Aebi, U., 1996. 3-D reconstructions from ice-embedded and negatively stained biomacromolecular assemblies: a critical comparison. J. Struct. Biol., 117, 99-116.
    • (1996) J. Struct. Biol. , vol.117 , pp. 99-116
    • Hoenger, A.1    Aebi, U.2
  • 29
    • 0016207970 scopus 로고
    • A negative staining-carbon film technique for studying viruses in the electron microscope. I. Preparation procedure for examining icosahedral and filamentous viruses
    • Horne, R. W. and Pasquali-Ronchetti, I., 1974. A negative staining-carbon film technique for studying viruses in the electron microscope. I. Preparation procedure for examining icosahedral and filamentous viruses. J. Ultrastruct. Res., 47, 361-383.
    • (1974) J. Ultrastruct. Res. , vol.47 , pp. 361-383
    • Horne, R.W.1    Pasquali-Ronchetti, I.2
  • 30
    • 0027112252 scopus 로고
    • CRISP: Crystallographic image processing on a personal computer
    • Hovmöller, S., 1992. CRISP: crystallographic image processing on a personal computer. Ultramicroscopy, 41, 121-135.
    • (1992) Ultramicroscopy , vol.41 , pp. 121-135
    • Hovmöller, S.1
  • 31
    • 0024961660 scopus 로고
    • Visualization of alpha-helices in tobacco mosaic virus by cryoelectron microscopy
    • Jeng, T. W., Crowther, R. A., Stubbs, G. and Chiu, W., 1989. Visualization of alpha-helices in tobacco mosaic virus by cryoelectron microscopy. J. Molec. Biol., 205, 251-257.
    • (1989) J. Molec. Biol. , vol.205 , pp. 251-257
    • Jeng, T.W.1    Crowther, R.A.2    Stubbs, G.3    Chiu, W.4
  • 32
    • 0027166044 scopus 로고
    • Virus accumulate spontaneously near droplet surfaces: A method to concentrate viruses for electron microscopy
    • Johnson, R. P. C. and Gregory, D. W., 1993. Virus accumulate spontaneously near droplet surfaces: a method to concentrate viruses for electron microscopy. J. Microsc., 171, 125-136.
    • (1993) J. Microsc. , vol.171 , pp. 125-136
    • Johnson, R.P.C.1    Gregory, D.W.2
  • 33
    • 0031454799 scopus 로고    scopus 로고
    • Utility of butvar support film and methylamine tungstate stain in three-dimensional electron microscopy: Agreement between stain and frozen-hydrated reconstructions
    • Kolodziej, S. J., Penczek, P. A. and Stoops, J. K., 1997. Utility of butvar support film and methylamine tungstate stain in three-dimensional electron microscopy: agreement between stain and frozen-hydrated reconstructions. J. Struct. Biol., 120, 158-167.
    • (1997) J. Struct. Biol. , vol.120 , pp. 158-167
    • Kolodziej, S.J.1    Penczek, P.A.2    Stoops, J.K.3
  • 34
    • 0000121165 scopus 로고
    • Activities of urease and pepsin monolayers
    • Langmuir, I. and Schaeffer, V. J., 1938. Activities of urease and pepsin monolayers. J. Amer. Chem. Soc., 60, 2829-2839.
    • (1938) J. Amer. Chem. Soc. , vol.60 , pp. 2829-2839
    • Langmuir, I.1    Schaeffer, V.J.2
  • 35
    • 0020691376 scopus 로고
    • Electron microscopy of frozen biological suspensions
    • Lepault, J., Booy, F. P. and Dubochet, J., 1983. Electron microscopy of frozen biological suspensions. J. Microsc., 129, 89-102.
    • (1983) J. Microsc. , vol.129 , pp. 89-102
    • Lepault, J.1    Booy, F.P.2    Dubochet, J.3
  • 36
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin type 1 (KLH) at 15 Å resolution by electron cryomicroscopy and angular reconstitution
    • Orlova, E., Dube, P., Harris, J. R., Beckman, E., Zemlin, F., Markl, J. and van Heel, M., 1997. Structure of keyhole limpet hemocyanin type 1 (KLH) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. J. Molec. Biol., 217, 417-437.
    • (1997) J. Molec. Biol. , vol.217 , pp. 417-437
    • Orlova, E.1    Dube, P.2    Harris, J.R.3    Beckman, E.4    Zemlin, F.5    Markl, J.6    Van Heel, M.7
  • 37
    • 0026719146 scopus 로고
    • Zero-loss energy-filtered imaging of frozen-hydrated proteins: Model calculations and implications for future developments
    • Schröder, R. R., 1992. Zero-loss energy-filtered imaging of frozen-hydrated proteins: model calculations and implications for future developments. J. Microsc., 166, 389-400.
    • (1992) J. Microsc. , vol.166 , pp. 389-400
    • Schröder, R.R.1
  • 38
    • 0025552735 scopus 로고
    • Zero-loss energy filtering as improved imaging mode in cryoelectron microscopy of frozen-hydrated specimens
    • Schröder, R. R., Hofmann, W. and Menetret, J.-F., 1990. Zero-loss energy filtering as improved imaging mode in cryoelectron microscopy of frozen-hydrated specimens. J. Struct. Biol., 105, 28-34.
    • (1990) J. Struct. Biol. , vol.105 , pp. 28-34
    • Schröder, R.R.1    Hofmann, W.2    Menetret, J.-F.3
  • 39
    • 0024990689 scopus 로고
    • Orientated crystallization as a tool for detecting ordered aggregates of water-soluble hydrophobic α-amino acids at air-solution interface
    • Weissbuch, I., Frolow, F., Addadi, L., Lahav, M. and Leiserowitz, L., 1990. Orientated crystallization as a tool for detecting ordered aggregates of water-soluble hydrophobic α-amino acids at air-solution interface. J. Amer. Chem. Soc., 112, 7718-7724.
    • (1990) J. Amer. Chem. Soc. , vol.112 , pp. 7718-7724
    • Weissbuch, I.1    Frolow, F.2    Addadi, L.3    Lahav, M.4    Leiserowitz, L.5
  • 40
    • 0019350676 scopus 로고
    • The formation of two-dimensional arrays of isometric plant viruses in the presence of polyethylene glycol
    • Wells, B., Horne, R. W. and Shaw, P. J., 1981. The formation of two-dimensional arrays of isometric plant viruses in the presence of polyethylene glycol. Micron, 12, 37-45.
    • (1981) Micron , vol.12 , pp. 37-45
    • Wells, B.1    Horne, R.W.2    Shaw, P.J.3


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