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Volumn 138, Issue 3, 2002, Pages 216-226

Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles

Author keywords

3D reconstruction; Beam damage; Cryo negative staining; Cryoelectron microscopy; Fitting; GroEL; Specimen preparation; Vitrification

Indexed keywords

CHAPERONIN; PROTEIN SUBUNIT;

EID: 0036427905     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00035-7     Document Type: Article
Times cited : (57)

References (41)
  • 3
    • 0027275623 scopus 로고
    • Three-dimensional architecture of human α2-macroglobulin transformed with methyl-amine
    • doi:10.1006/jmbi.1993.1408
    • Boisset, N., Penczek, P., Pochon, F., Frank, J., Lamy, J.N., 1993. Three-dimensional architecture of human α2-macroglobulin transformed with methyl-amine. J. Mol. Biol. 232, 522-529, doi:10.1006/jmbi.1993.1408.
    • (1993) J. Mol. Biol. , vol.232 , pp. 522-529
    • Boisset, N.1    Penczek, P.2    Pochon, F.3    Frank, J.4    Lamy, J.N.5
  • 4
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig, K., Adams, P.D., Brunger, A.T., 1995. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol. 2, 1083-1094.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brunger, A.T.3
  • 5
    • 0001644632 scopus 로고
    • Between objectivity and subjectivity
    • Brändén, C.I., Jones, T.A., 1990. Between objectivity and subjectivity. Nature 343, 687-689.
    • (1990) Nature , vol.343 , pp. 687-689
    • Brändén, C.I.1    Jones, T.A.2
  • 6
    • 0026499357 scopus 로고
    • Has negative staining a future in biomolecular electron microscopy?
    • Bremer, A., Hann, C., Engel, A., Baumeister, W., Aebi, U., 1992. Has negative staining a future in biomolecular electron microscopy? Ultramicroscopy 46, 85-111.
    • (1992) Ultramicroscopy , vol.46 , pp. 85-111
    • Bremer, A.1    Hann, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 7
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner, S., Horne, R.W., 1959. A negative staining method for high resolution electron microscopy of viruses. Bioch. Biophys. Acta 34, 60-71.
    • (1959) Bioch. Biophys. Acta , vol.34 , pp. 60-71
    • Brenner, S.1    Horne, R.W.2
  • 8
    • 0026852571 scopus 로고
    • Fast rigid-body refinement for molecular replacement techniques
    • Castellano, E., Oliva, G., Navaza, J., 1992. Fast rigid-body refinement for molecular replacement techniques. J. Appl. Cryst. 25, 281-284.
    • (1992) J. Appl. Cryst. , vol.25 , pp. 281-284
    • Castellano, E.1    Oliva, G.2    Navaza, J.3
  • 9
    • 0033372028 scopus 로고    scopus 로고
    • Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution
    • doi:10.1006/jsbi.1999.4168
    • Conway, J.F., Steven, A.C., 1999. Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution. J. Struct. Biol. 128, 106-118, doi:10.1006/jsbi.1999.4168.
    • (1999) J. Struct. Biol. , vol.128 , pp. 106-118
    • Conway, J.F.1    Steven, A.C.2
  • 10
    • 0027853061 scopus 로고
    • The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids
    • doi:10.1006/jsbi.1993.1052
    • Conway, J.F., Trus, B.L., Booy, F.P., Newcomb, W.W., Brown, J.C., Steven, A.C., 1993. The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids. J. Struct. Biol. 111, 222-233, doi:10.1006/jsbi.1993.1052.
    • (1993) J. Struct. Biol. , vol.111 , pp. 222-233
    • Conway, J.F.1    Trus, B.L.2    Booy, F.P.3    Newcomb, W.W.4    Brown, J.C.5    Steven, A.C.6
  • 13
    • 0034972451 scopus 로고    scopus 로고
    • Structural changes in GroEL effected by binding a denaturated protein substrate
    • doi:10.1006/jmbi.2001.4613
    • Falke, S., Fisher, M.T., Gogol, E.P., 2001. Structural changes in GroEL effected by binding a denaturated protein substrate. J. Mol. Biol. 308, 569-577, doi:10.1006/jmbi.2001.4613.
    • (2001) J. Mol. Biol. , vol.308 , pp. 569-577
    • Falke, S.1    Fisher, M.T.2    Gogol, E.P.3
  • 15
    • 0029975088 scopus 로고
    • Spider and Web: Processing and visualization of images in 3-D electron microscopy and related fields
    • doi:10.1006/jsbi.1996.0030
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., 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, doi:10.1006/jsbi.1996.0030.
    • (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
  • 16
    • 0015106320 scopus 로고
    • Limitations to significant information in biological electron microscopy as a result of radiation damage
    • Glaeser, R.M., 1971. Limitations to significant information in biological electron microscopy as a result of radiation damage. J. Ultrastruct. Res. 36, 466-482.
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 466-482
    • Glaeser, R.M.1
  • 17
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz, G., van Heel, M., 1986. Exact filters for general geometry three dimensional reconstruction. Optik 73, 146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    Van Heel, M.2
  • 18
    • 0001439498 scopus 로고
    • Negative staining
    • Harris, J.R. (Ed.). Oxford Univ. Press, Oxford
    • Harris, J.R., Horne, R.W., 1991. Negative staining. In: Harris, J.R. (Ed.), Electron Microscopy in Biology. Oxford Univ. Press, Oxford.
    • (1991) Electron Microscopy in Biology
    • Harris, J.R.1    Horne, R.W.2
  • 19
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl, M.K., Weber, F., Hartl, F.U., 1996. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 15, 6111-6121.
    • (1996) EMBO J. , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 20
    • 0026523919 scopus 로고
    • Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice
    • Henderson, R., 1992. Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicroscopy 46, 1-18.
    • (1992) Ultramicroscopy , vol.46 , pp. 1-18
    • Henderson, R.1
  • 21
    • 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. Q. Rev. Biophys. 28, 171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 22
    • 84985294851 scopus 로고
    • Quantitative assessment of radiation damage in a thin protein crystal
    • Jeng, T.-W., Chiu, W., 1984. Quantitative assessment of radiation damage in a thin protein crystal. J. Microsc. 136, 35-44.
    • (1984) J. Microsc. , vol.136 , pp. 35-44
    • Jeng, T.-W.1    Chiu, W.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr Sect. A 47, 110-119.
    • (1991) Acta Crystallogr Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0029123968 scopus 로고
    • Cryoelectron energy loss spectroscopy: Observation on vitrified hydrated specimens and radiation damage
    • Leapman, R.D., Sun, S., 1995. Cryoelectron energy loss spectroscopy: Observation on vitrified hydrated specimens and radiation damage. Ultramicroscopy 59, 71-79.
    • (1995) Ultramicroscopy , vol.59 , pp. 71-79
    • Leapman, R.D.1    Sun, S.2
  • 25
    • 0020691376 scopus 로고
    • Electron microscopy of frozen biological suspensions
    • Lepault, J., Booy, F.P., 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
  • 26
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • doi:10.1006/jmbi.2001.5077
    • Lowe, J., Downing, K.H., Nogales, E., 2001. Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057, doi:10.1006/jmbi.2001.5077.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Lowe, J.1    Downing, K.H.2    Nogales, E.3
  • 27
    • 0032967642 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor at 4.6 Å resolution: Transverse tunnels in the channel wall
    • doi:10.1006/jmbi.1999.2721
    • Miyazawa, A., Fujiyoshi, Y., Stowell, M., Unwin, N., 1999. Nicotinic acetylcholine receptor at 4.6 Åresolution: Transverse tunnels in the channel wall. J. Mol. Biol. 288, 765-786, doi:10.1006/jmbi.1999.2721.
    • (1999) J. Mol. Biol. , vol.288 , pp. 765-786
    • Miyazawa, A.1    Fujiyoshi, Y.2    Stowell, M.3    Unwin, N.4
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J., 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr. Sect. A 50, 157-163.
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution
    • doi:10.1006/jmbi.1997.1182
    • Orlova, E.V., Dube, P., Harris, J.R., Beckman, E., Zemlin, F., Marlk, J., vanHeel, M., 1997. Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. J. Mol. Biol. 271, 417-437, doi:10.1006/jmbi.1997.1182.
    • (1997) J. Mol. Biol. , vol.271 , pp. 417-437
    • Orlova, E.V.1    Dube, P.2    Harris, J.R.3    Beckman, E.4    Zemlin, F.5    Marlk, J.6    VanHeel, M.7
  • 30
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles
    • Penczek, P., Grassucci, R.A., Frank, J., 1994. The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryoelectron microscopy of biological particles. Ultramicroscopy 53, 251-270.
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.1    Grassucci, R.A.2    Frank, J.3
  • 31
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman, A.M., Chen, S., White, H., Braig, K., Saibil, H.R., 1996. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87, 241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 32
    • 0035783162 scopus 로고    scopus 로고
    • Structures of unliganded and ATP-bound states of the E. coli chaperonin GroEL by cryoelectron microscopy
    • doi:10.1006/jsbi.2001.4374
    • Roseman, A.R., Ranson, N.A., Gowen, B., Fuller, S.D., Saibil, H.R., 2001. Structures of unliganded and ATP-bound states of the E. coli chaperonin GroEL by cryoelectron microscopy. J. Struct. Biol. 135, 115-125, doi:10.1006/jsbi.2001.4374.
    • (2001) J. Struct. Biol. , vol.135 , pp. 115-125
    • Roseman, A.R.1    Ranson, N.A.2    Gowen, B.3    Fuller, S.D.4    Saibil, H.R.5
  • 33
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye, H.S., Roseman, A.M., Chen, S., Furtak, K., Fenton, W.A., Saibil, H.R., Horwich, A.L., 1999. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97, 325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 35
    • 84985234385 scopus 로고
    • Electron beam radiation damage to organic inclusions in vitreous, cubic and hexagonal ice
    • Talmon, Y., Adrian, M., Dubochet, J., 1986. Electron beam radiation damage to organic inclusions in vitreous, cubic and hexagonal ice. J. Microsc. 141, 375-384.
    • (1986) J. Microsc. , vol.141 , pp. 375-384
    • Talmon, Y.1    Adrian, M.2    Dubochet, J.3
  • 36
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor, K.A., Glaeser, R.M., 1974. Electron diffraction of frozen, hydrated protein crystals. Science 186, 1036-1037.
    • (1974) Science , vol.186 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 37
    • 0016299061 scopus 로고
    • Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein. II. The influence of electron irradiation of the stain distribution
    • Unwin, N., 1974. Electron microscopy of the stacked disk aggregate of tobacco mosaic virus protein. II. The influence of electron irradiation of the stain distribution. J. Mol. Biol. 87, 657-670.
    • (1974) J. Mol. Biol. , vol.87 , pp. 657-670
    • Unwin, N.1
  • 38
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signal-to-noise ratios
    • Unser, M., Trus, B.L., Steven, A.C., 1987. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicroscopy 23, 39-52.
    • (1987) Ultramicroscopy , vol.23 , pp. 39-52
    • Unser, M.1    Trus, B.L.2    Steven, A.C.3
  • 39
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel, M., 1987. Similarity measures between images. Ultramicroscopy 21, 95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 41
    • 0030960710 scopus 로고    scopus 로고
    • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: Procedure and application to the 70S Escherichia coli ribosome
    • doi:10.1006/jsbi.1997.3845
    • Zhu, J., Penczek, P.A., Schröder, R.R., Frank, J., 1997. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: Procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 118, 197-219, doi:10.1006/jsbi.1997.3845.
    • (1997) J. Struct. Biol. , vol.118 , pp. 197-219
    • Zhu, J.1    Penczek, P.A.2    Schröder, R.R.3    Frank, J.4


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