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Volumn 96, Issue C, 2010, Pages 21-45

Bacterial TEM. New insights from cryo-microscopy

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 77956992845     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(10)96002-0     Document Type: Book
Times cited : (65)

References (105)
  • 2
    • 15444366581 scopus 로고    scopus 로고
    • Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy
    • Al-Amoudi A., Studer D., Dubochet J. Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy. J. Struct. Biol. 2005, 150:109-121.
    • (2005) J. Struct. Biol. , vol.150 , pp. 109-121
    • Al-Amoudi, A.1    Studer, D.2    Dubochet, J.3
  • 5
    • 0016138373 scopus 로고
    • Ultrastructure and organization of the bacterial envelope
    • Bayer M.E. Ultrastructure and organization of the bacterial envelope. Ann. NY. Acad. Sci. 1974, 235:6-28.
    • (1974) Ann. NY. Acad. Sci. , vol.235 , pp. 6-28
    • Bayer, M.E.1
  • 8
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E., Lutkenhaus J. FtsZ ring structure associated with division in Escherichia coli. Nature 1991, 354:161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.1    Lutkenhaus, J.2
  • 9
    • 60349116495 scopus 로고    scopus 로고
    • Cryoelectron microscopy of vitreous sections: A step further towards the native state
    • Bouchet-Marquis C., Fakan S. Cryoelectron microscopy of vitreous sections: A step further towards the native state. Methods Mol. Biol. 2009, 464:425-439.
    • (2009) Methods Mol. Biol. , vol.464 , pp. 425-439
    • Bouchet-Marquis, C.1    Fakan, S.2
  • 11
    • 70350126125 scopus 로고    scopus 로고
    • Universal architecture of bacterial chemoreceptor arrays
    • Briegel A., et al. Universal architecture of bacterial chemoreceptor arrays. Proc Natl. Acad. Sci. U. S.A. 2009, 106:17181-17186.
    • (2009) Proc Natl. Acad. Sci. U. S.A. , vol.106 , pp. 17181-17186
    • Briegel, A.1
  • 12
    • 33748670272 scopus 로고    scopus 로고
    • Multiple large filament bundles observed in Caulobacter crescentus by electron cryotomography
    • Briegel A., Dias D.P., Li Z., Jensen R.B., Frangakis A.S., Jensen G.J. Multiple large filament bundles observed in Caulobacter crescentus by electron cryotomography. Mol. Microbiol. 2006, 62:5-14.
    • (2006) Mol. Microbiol. , vol.62 , pp. 5-14
    • Briegel, A.1    Dias, D.P.2    Li, Z.3    Jensen, R.B.4    Frangakis, A.S.5    Jensen, G.J.6
  • 14
    • 0026327509 scopus 로고
    • Localization of outer surface proteins A and B in both the outer membrane and intracellular compartments of Borrelia burgdorferi
    • Brusca J.S., McDowall A.W., Norgard M.V., Radolf J.D. Localization of outer surface proteins A and B in both the outer membrane and intracellular compartments of Borrelia burgdorferi. J. Bacteriol. 1991, 173:8004-8008.
    • (1991) J. Bacteriol. , vol.173 , pp. 8004-8008
    • Brusca, J.S.1    McDowall, A.W.2    Norgard, M.V.3    Radolf, J.D.4
  • 15
    • 0343145412 scopus 로고
    • Electron microscopy of ultra-thin sections of bacteria I. Cellular division in bacillus cereus
    • Chapman G.B., Hillier J. Electron microscopy of ultra-thin sections of bacteria I. Cellular division in bacillus cereus. J. Bacteriol. 1953, 66:362-373.
    • (1953) J. Bacteriol. , vol.66 , pp. 362-373
    • Chapman, G.B.1    Hillier, J.2
  • 16
    • 28944435740 scopus 로고    scopus 로고
    • Dose tolerance at helium and nitrogen temperatures for whole cell electron tomography
    • Comolli L.R., Downing K.H. Dose tolerance at helium and nitrogen temperatures for whole cell electron tomography. J. Struct. Biol. 2005, 152:149-156.
    • (2005) J. Struct. Biol. , vol.152 , pp. 149-156
    • Comolli, L.R.1    Downing, K.H.2
  • 17
    • 33745830137 scopus 로고    scopus 로고
    • Characterization of intact subcellular bodies in whole bacteria by cryo-electron tomography and spectroscopic imaging
    • Comolli L.R., Kundmann M., Downing K.H. Characterization of intact subcellular bodies in whole bacteria by cryo-electron tomography and spectroscopic imaging. J. Microsc. 2006, 223:40-52.
    • (2006) J. Microsc. , vol.223 , pp. 40-52
    • Comolli, L.R.1    Kundmann, M.2    Downing, K.H.3
  • 19
    • 59149094180 scopus 로고    scopus 로고
    • Visualization of proteins in intact cells with a clonable tag for electron microscopy
    • Diestra E., Fontana J., Guichard P., Marco S., Risco C. Visualization of proteins in intact cells with a clonable tag for electron microscopy. J. Struct. Biol. 2008, 165:157-168.
    • (2008) J. Struct. Biol. , vol.165 , pp. 157-168
    • Diestra, E.1    Fontana, J.2    Guichard, P.3    Marco, S.4    Risco, C.5
  • 22
    • 0019836642 scopus 로고
    • Vitrification of pure water for electron microscopy
    • RP
    • Dubochet J., McDowall A.W. Vitrification of pure water for electron microscopy. J. Microsc. 1981, 124. RP.
    • (1981) J. Microsc. , vol.124
    • Dubochet, J.1    McDowall, A.W.2
  • 24
    • 0019421611 scopus 로고
    • Nucleoid structure in freeze fractures of streptococcus faecalis: Effects of filtration and chilling
    • Edelstein E., Parks L., Tsien H.C., Daneo-Moore L., Higgins M.L. Nucleoid structure in freeze fractures of streptococcus faecalis: Effects of filtration and chilling. J. Bacteriol. 1981, 146:798-803.
    • (1981) J. Bacteriol. , vol.146 , pp. 798-803
    • Edelstein, E.1    Parks, L.2    Tsien, H.C.3    Daneo-Moore, L.4    Higgins, M.L.5
  • 25
    • 28044437733 scopus 로고    scopus 로고
    • Fine structure of the Deinococcus radiodurans nucleoid revealed by cryoelectron microscopy of vitreous sections
    • Eltsov M., Dubochet J. Fine structure of the Deinococcus radiodurans nucleoid revealed by cryoelectron microscopy of vitreous sections. J. Bacteriol. 2005, 187:8047-8054.
    • (2005) J. Bacteriol. , vol.187 , pp. 8047-8054
    • Eltsov, M.1    Dubochet, J.2
  • 26
    • 33748993717 scopus 로고    scopus 로고
    • Study of the Deinococcus radiodurans nucleoid by cryoelectron microscopy of vitreous sections: Supplementary comments
    • Eltsov M., Dubochet J. Study of the Deinococcus radiodurans nucleoid by cryoelectron microscopy of vitreous sections: Supplementary comments. J. Bacteriol. 2006, 188:6053-6058.
    • (2006) J. Bacteriol. , vol.188 , pp. 6053-6058
    • Eltsov, M.1    Dubochet, J.2
  • 27
    • 33750526675 scopus 로고    scopus 로고
    • Transmission electron microscopy of the bacterial nucleoid
    • Eltsov M., Zuber B. Transmission electron microscopy of the bacterial nucleoid. J. Struct. Biol. 2006, 156:246-254.
    • (2006) J. Struct. Biol. , vol.156 , pp. 246-254
    • Eltsov, M.1    Zuber, B.2
  • 28
    • 0031919894 scopus 로고    scopus 로고
    • Electron microscopy of frozen biological objects: A study using cryosectioning and cryosubstitution
    • Erk I., Nicolas G., Caroff A., Lepault J. Electron microscopy of frozen biological objects: A study using cryosectioning and cryosubstitution. J. Microsc. 1998, 189:236-248.
    • (1998) J. Microsc. , vol.189 , pp. 236-248
    • Erk, I.1    Nicolas, G.2    Caroff, A.3    Lepault, J.4
  • 29
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis A.S., Hegerl R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 2001, 135:239-250.
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 30
    • 13844298720 scopus 로고    scopus 로고
    • Cryoelectron microscopy of liposomes
    • Frederik P.M., Hubert D.H. Cryoelectron microscopy of liposomes. Methods Enzymol. 2005, 391:431-448.
    • (2005) Methods Enzymol. , vol.391 , pp. 431-448
    • Frederik, P.M.1    Hubert, D.H.2
  • 31
    • 0035225444 scopus 로고    scopus 로고
    • Using rapid freeze and freeze-substitution for the preparation of yeast cells for electron microscopy and three-dimensional analysis
    • Giddings T.H., O'Toole E.T., Morphew M., Mastronarde D.N., McIntosh J.R., Winey M. Using rapid freeze and freeze-substitution for the preparation of yeast cells for electron microscopy and three-dimensional analysis. Methods Cell Biol. 2001, 67:27-42.
    • (2001) Methods Cell Biol. , vol.67 , pp. 27-42
    • Giddings, T.H.1    O'Toole, E.T.2    Morphew, M.3    Mastronarde, D.N.4    McIntosh, J.R.5    Winey, M.6
  • 32
    • 33750521659 scopus 로고
    • Zur organisation des zellkerns von Bacillus megaterium
    • Giesbrecht P., Piekarski G. Zur organisation des zellkerns von Bacillus megaterium. Arch. Mikrobiol. 1958, 31:68-81.
    • (1958) Arch. Mikrobiol. , vol.31 , pp. 68-81
    • Giesbrecht, P.1    Piekarski, G.2
  • 33
    • 0026479698 scopus 로고
    • Freeze-substitution studies of bacteria
    • Graham L.L. Freeze-substitution studies of bacteria. Electron Microsc. Rev. 1992, 5:77-103.
    • (1992) Electron Microsc. Rev. , vol.5 , pp. 77-103
    • Graham, L.L.1
  • 34
    • 0016662064 scopus 로고
    • Mesosomes: membranous bacterial organelles
    • Greenawalt J.W., Whiteside T.L. Mesosomes: membranous bacterial organelles. Bacteriol. Rev. 1975, 39:405-463.
    • (1975) Bacteriol. Rev. , vol.39 , pp. 405-463
    • Greenawalt, J.W.1    Whiteside, T.L.2
  • 35
    • 0017107814 scopus 로고
    • Organization of mesosomes in fixed and unfixed cells
    • Higgins M.L., Tsien H.C., Daneo-Moore L. Organization of mesosomes in fixed and unfixed cells. J. Bacteriol. 1976, 127:1519-1523.
    • (1976) J. Bacteriol. , vol.127 , pp. 1519-1523
    • Higgins, M.L.1    Tsien, H.C.2    Daneo-Moore, L.3
  • 36
    • 0021796303 scopus 로고
    • Shape and fine structure of nucleoids observed on sections of ultrarapidly frozen and cryosubstituted bacteria
    • Hobot J.A., Villiger W., Escaig J., Maeder M., Ryter A., Kellenberger E. Shape and fine structure of nucleoids observed on sections of ultrarapidly frozen and cryosubstituted bacteria. J. Bacteriol. 1985, 162:960-971.
    • (1985) J. Bacteriol. , vol.162 , pp. 960-971
    • Hobot, J.A.1    Villiger, W.2    Escaig, J.3    Maeder, M.4    Ryter, A.5    Kellenberger, E.6
  • 37
    • 69249126071 scopus 로고    scopus 로고
    • Freeze-substitution
    • CRC Press, Boca Raton, A. Cavalier, D. Spehner, B.M. Humbel (Eds.)
    • Humbel B.M. Freeze-substitution. Handbook of Cryo-Preparation Methods for Electron Microscopy 2009, 319-341. CRC Press, Boca Raton. A. Cavalier, D. Spehner, B.M. Humbel (Eds.).
    • (2009) Handbook of Cryo-Preparation Methods for Electron Microscopy , pp. 319-341
    • Humbel, B.M.1
  • 38
    • 0035970279 scopus 로고    scopus 로고
    • In situ localization of beta-glucans in the cell wall of Schizosaccharomyces pombe
    • Humbel B.M., Konomi M., Takagi T., Kamasawa N., Ishijima S.A., Osumi M. In situ localization of beta-glucans in the cell wall of Schizosaccharomyces pombe. Yeast 2001, 18:433-444.
    • (2001) Yeast , vol.18 , pp. 433-444
    • Humbel, B.M.1    Konomi, M.2    Takagi, T.3    Kamasawa, N.4    Ishijima, S.A.5    Osumi, M.6
  • 39
    • 34147099837 scopus 로고    scopus 로고
    • Electron cryotomography sample preparation using the vitrobot
    • Iancu C.V., et al. Electron cryotomography sample preparation using the vitrobot. Nat. Protoc. 2006, 1:2813-2819.
    • (2006) Nat. Protoc. , vol.1 , pp. 2813-2819
    • Iancu, C.V.1
  • 40
    • 74649083831 scopus 로고    scopus 로고
    • Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells
    • Iancu C.V., Morris D.M., Dou Z., Heinhorst S., Cannon G.C., Jensen G.J. Organization, structure, and assembly of alpha-carboxysomes determined by electron cryotomography of intact cells. J. Mol. Biol. 2010, 396:105-117.
    • (2010) J. Mol. Biol. , vol.396 , pp. 105-117
    • Iancu, C.V.1    Morris, D.M.2    Dou, Z.3    Heinhorst, S.4    Cannon, G.C.5    Jensen, G.J.6
  • 42
    • 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., Jensen G.J. A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography. J. Struct. Biol. 2006, 153:231-240.
    • (2006) J. Struct. Biol. , vol.153 , pp. 231-240
    • Iancu, C.V.1    Wright, E.R.2    Heymann, J.B.3    Jensen, G.J.4
  • 44
    • 69249084367 scopus 로고    scopus 로고
    • BAL-TEC HPM 010high-pressure freezing machine
    • CRC Press, Boca Raton, A. Cavalier, D. Spehner, B.M. Humbel (Eds.)
    • Kaech A. BAL-TEC HPM 010high-pressure freezing machine. Handbook of Cryo-Preparation Methods for Electron Microscopy 2009, 101-128. CRC Press, Boca Raton. A. Cavalier, D. Spehner, B.M. Humbel (Eds.).
    • (2009) Handbook of Cryo-Preparation Methods for Electron Microscopy , pp. 101-128
    • Kaech, A.1
  • 45
    • 0026685334 scopus 로고
    • Chromatins of low-protein content: Special features of their compaction and condensation
    • Kellenberger E., Arnold-Schulz-Gahmen B. Chromatins of low-protein content: Special features of their compaction and condensation. FEMS Microbiol. Lett. 1992, 79:361-370.
    • (1992) FEMS Microbiol. Lett. , vol.79 , pp. 361-370
    • Kellenberger, E.1    Arnold-Schulz-Gahmen, B.2
  • 46
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili A., Li Z., Newman D.K., Jensen G.J. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 2006, 311:242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 47
    • 70849132924 scopus 로고    scopus 로고
    • Proteome organization in a genome-reduced bacterium
    • Kuhner S., et al. Proteome organization in a genome-reduced bacterium. Science 2009, 326:1235-1240.
    • (2009) Science , vol.326 , pp. 1235-1240
    • Kuhner, S.1
  • 48
    • 33847186592 scopus 로고    scopus 로고
    • Electron tomography of immunolabeled cryosections
    • Ladinsky M.S., Howell K.E. Electron tomography of immunolabeled cryosections. Methods Cell Biol. 2007, 79:543-558.
    • (2007) Methods Cell Biol. , vol.79 , pp. 543-558
    • Ladinsky, M.S.1    Howell, K.E.2
  • 49
    • 33845790956 scopus 로고    scopus 로고
    • Vitreous cryo-sectioning of cells facilitated by a micromanipulator
    • Ladinsky M.S., Pierson J.M., McIntosh J.R. Vitreous cryo-sectioning of cells facilitated by a micromanipulator. J. Microsc. 2006, 224:129-134.
    • (2006) J. Microsc. , vol.224 , pp. 129-134
    • Ladinsky, M.S.1    Pierson, J.M.2    McIntosh, J.R.3
  • 51
    • 9744252288 scopus 로고    scopus 로고
    • Bacterial subcellular architecture: Recent advances and future prospects
    • Lewis P.J. Bacterial subcellular architecture: Recent advances and future prospects. Mol. Microbiol. 2004, 54:1135-1150.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1135-1150
    • Lewis, P.J.1
  • 52
    • 66349121016 scopus 로고    scopus 로고
    • Electron cryotomography: A new view into microbial ultrastructure
    • Li Z., Jensen G.J. Electron cryotomography: A new view into microbial ultrastructure. Curr. Opin. Microbiol. 2009, 12:333-340.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 333-340
    • Li, Z.1    Jensen, G.J.2
  • 53
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z., Trimble M.J., Brun Y.V., Jensen G.J. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 2007, 26:4694-4708.
    • (2007) EMBO J. , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 54
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou W., Geuze H.J., Slot J.W. Improving structural integrity of cryosections for immunogold labeling. Histochem. Cell. Biol. 1996, 106:41-58.
    • (1996) Histochem. Cell. Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 55
    • 67749093018 scopus 로고    scopus 로고
    • Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: Evidence for stator ring curvature and rotor/C ring assembly flexion
    • Liu J., Lin T., Botkin D.J., McCrum E., Winkler H., Norris S.J. Intact flagellar motor of Borrelia burgdorferi revealed by cryo-electron tomography: Evidence for stator ring curvature and rotor/C ring assembly flexion. J. Bacteriol. 2009, 191:5026-5036.
    • (2009) J. Bacteriol. , vol.191 , pp. 5026-5036
    • Liu, J.1    Lin, T.2    Botkin, D.J.3    McCrum, E.4    Winkler, H.5    Norris, S.J.6
  • 56
    • 0034005546 scopus 로고    scopus 로고
    • Green fluorescent protein as a reporter for macromolecular localization in bacterial cells
    • Margolin W. Green fluorescent protein as a reporter for macromolecular localization in bacterial cells. Methods 2000, 20:62-72.
    • (2000) Methods , vol.20 , pp. 62-72
    • Margolin, W.1
  • 57
    • 33845766325 scopus 로고    scopus 로고
    • Deep-etching electron microscopy of cells of Magnetospirillum magnetotacticum: Evidence for filamentous structures connecting the magnetosome chain to the cell surface
    • Martins J.L., Keim C.N., Farina M., Kachar B., Lins U. Deep-etching electron microscopy of cells of Magnetospirillum magnetotacticum: Evidence for filamentous structures connecting the magnetosome chain to the cell surface. Curr. Microbiol. 2007, 54:1-4.
    • (2007) Curr. Microbiol. , vol.54 , pp. 1-4
    • Martins, J.L.1    Keim, C.N.2    Farina, M.3    Kachar, B.4    Lins, U.5
  • 58
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 2005, 152:36-51.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 59
    • 42649136218 scopus 로고    scopus 로고
    • Correction for non-perpendicularity of beam and tilt axis in tomographic reconstructions with the IMOD package
    • Mastronarde D.N. Correction for non-perpendicularity of beam and tilt axis in tomographic reconstructions with the IMOD package. J. Microsc. 2008, 230:212-217.
    • (2008) J. Microsc. , vol.230 , pp. 212-217
    • Mastronarde, D.N.1
  • 60
    • 11144311269 scopus 로고    scopus 로고
    • Inactivation of swmA results in the loss of an outer cell layer in a swimming synechococcus strain
    • McCarren J., Heuser J., Roth R., Yamada N., Martone M., Brahamsha B. Inactivation of swmA results in the loss of an outer cell layer in a swimming synechococcus strain. J. Bacteriol. 2005, 187:224-230.
    • (2005) J. Bacteriol. , vol.187 , pp. 224-230
    • McCarren, J.1    Heuser, J.2    Roth, R.3    Yamada, N.4    Martone, M.5    Brahamsha, B.6
  • 61
    • 33847186352 scopus 로고    scopus 로고
    • Recent advances in high-pressure freezing: Equipment- and specimen-loading methods
    • McDonald K.L., Morphew M., Verkade P., Muller-Reichert T. Recent advances in high-pressure freezing: Equipment- and specimen-loading methods. Methods Mol. Biol. 2007, 369:143-173.
    • (2007) Methods Mol. Biol. , vol.369 , pp. 143-173
    • McDonald, K.L.1    Morphew, M.2    Verkade, P.3    Muller-Reichert, T.4
  • 62
    • 0020960227 scopus 로고
    • Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples
    • McDowall A.W., Chang J.J., Freeman R., Lepault J., Walter C.A., Dubochet J. Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples. J. Microsc. 1983, 131:1-9.
    • (1983) J. Microsc. , vol.131 , pp. 1-9
    • McDowall, A.W.1    Chang, J.J.2    Freeman, R.3    Lepault, J.4    Walter, C.A.5    Dubochet, J.6
  • 63
    • 34548627873 scopus 로고    scopus 로고
    • Concatenated metallothionein as a clonable gold label for electron microscopy
    • Mercogliano C., DeRosier D. Concatenated metallothionein as a clonable gold label for electron microscopy. J. Struct. Biol. 2007, 160:70-82.
    • (2007) J. Struct. Biol. , vol.160 , pp. 70-82
    • Mercogliano, C.1    DeRosier, D.2
  • 64
    • 69249213558 scopus 로고    scopus 로고
    • Cryo-electron tomography of bacteria: Progress, challenges and future prospects
    • Milne J.L., Subramaniam S. Cryo-electron tomography of bacteria: Progress, challenges and future prospects. Nat. Rev. Microbiol. 2009, 7:666-675.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 666-675
    • Milne, J.L.1    Subramaniam, S.2
  • 65
    • 0014355321 scopus 로고
    • Structural features of mesosomes (chondrioids) of Bacillus subtilis after freeze-etching
    • Nanninga N. Structural features of mesosomes (chondrioids) of Bacillus subtilis after freeze-etching. J. Cell Biol. 1968, 39:251-263.
    • (1968) J. Cell Biol. , vol.39 , pp. 251-263
    • Nanninga, N.1
  • 66
    • 0014707732 scopus 로고
    • Ultrastructure of the cell envelope of Escherichia coli B after freeze-etching
    • Nanninga N. Ultrastructure of the cell envelope of Escherichia coli B after freeze-etching. J. Bacteriol. 1970, 101:297-303.
    • (1970) J. Bacteriol. , vol.101 , pp. 297-303
    • Nanninga, N.1
  • 69
    • 0037288048 scopus 로고    scopus 로고
    • Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography
    • Nickell S., Hegerl R., Baumeister W., Rachel R. Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography. J. Struct. Biol. 2003, 141:34-42.
    • (2003) J. Struct. Biol. , vol.141 , pp. 34-42
    • Nickell, S.1    Hegerl, R.2    Baumeister, W.3    Rachel, R.4
  • 70
    • 35948943072 scopus 로고    scopus 로고
    • A genetically encoded metallothionein tag enabling efficient protein detection by electron microscopy
    • Nishino Y., Yasunaga T., Miyazawa A. A genetically encoded metallothionein tag enabling efficient protein detection by electron microscopy. J. Electron Microsc. 2007, 56:93-101.
    • (2007) J. Electron Microsc. , vol.56 , pp. 93-101
    • Nishino, Y.1    Yasunaga, T.2    Miyazawa, A.3
  • 71
    • 33750527990 scopus 로고    scopus 로고
    • Mapping 70s ribosomes in intact cells by cryoelectron tomography and pattern recognition
    • Ortiz J.O., Förster F., Kürner J., Linaroudis A.A., Baumeister W. Mapping 70s ribosomes in intact cells by cryoelectron tomography and pattern recognition. J. Struct. Biol. 2006, 156:334-341.
    • (2006) J. Struct. Biol. , vol.156 , pp. 334-341
    • Ortiz, J.O.1    Förster, F.2    Kürner, J.3    Linaroudis, A.A.4    Baumeister, W.5
  • 72
    • 0026655895 scopus 로고
    • Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols
    • Paul T.R., Beveridge T.J. Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols. J. Bacteriol. 1992, 174:6508-6517.
    • (1992) J. Bacteriol. , vol.174 , pp. 6508-6517
    • Paul, T.R.1    Beveridge, T.J.2
  • 73
    • 0028327368 scopus 로고
    • Preservation of surface lipids and determination of ultrastructure of Mycobacterium kansasii by freeze-substitution
    • Paul T.R., Beveridge T.J. Preservation of surface lipids and determination of ultrastructure of Mycobacterium kansasii by freeze-substitution. Infect. Immun. 1994, 62:1542-1550.
    • (1994) Infect. Immun. , vol.62 , pp. 1542-1550
    • Paul, T.R.1    Beveridge, T.J.2
  • 74
    • 74449094003 scopus 로고    scopus 로고
    • Improving the technique of vitreous cryo-sectioning for cryo-electron tomography: Electrostatic charging for section attachment and implementation of an anti-contamination glove box
    • Pierson J., Fernandez J.J., Bos E., Amini S., Gnaegi H., Vos M., Bel B., Adolfsen F., Carrascosa J.L., Peters P.J. Improving the technique of vitreous cryo-sectioning for cryo-electron tomography: Electrostatic charging for section attachment and implementation of an anti-contamination glove box. J. Struct. Biol. 2010, 169:219-225.
    • (2010) J. Struct. Biol. , vol.169 , pp. 219-225
    • Pierson, J.1    Fernandez, J.J.2    Bos, E.3    Amini, S.4    Gnaegi, H.5    Vos, M.6    Bel, B.7    Adolfsen, F.8    Carrascosa, J.L.9    Peters, P.J.10
  • 75
    • 36749101927 scopus 로고    scopus 로고
    • Characterization of bacterial operons consisting of two tubulins and a kinesin-like gene by the novel two-step gene walking method
    • Pilhofer M., Bauer A.P., Schrallhammer M., Richter L., Ludwig W., Schleifer K.H., Petroni G. Characterization of bacterial operons consisting of two tubulins and a kinesin-like gene by the novel two-step gene walking method. Nucleic Acids Res. 2007, 35:e135.
    • (2007) Nucleic Acids Res. , vol.35
    • Pilhofer, M.1    Bauer, A.P.2    Schrallhammer, M.3    Richter, L.4    Ludwig, W.5    Schleifer, K.H.6    Petroni, G.7
  • 77
    • 51549110953 scopus 로고    scopus 로고
    • A visualization and segmentation toolbox for electron microscopy
    • Pruggnaller S., Mayr M., Frangakis A. A visualization and segmentation toolbox for electron microscopy. J. Struct. Biol. 2008, 164:161-165.
    • (2008) J. Struct. Biol. , vol.164 , pp. 161-165
    • Pruggnaller, S.1    Mayr, M.2    Frangakis, A.3
  • 78
    • 2642680890 scopus 로고
    • Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum
    • Radolf J.D., Norgard M.V., Schulz W.W. Outer membrane ultrastructure explains the limited antigenicity of virulent Treponema pallidum. Proc. Natl. Acad. Sci. U. S.A. 1989, 86:2051-2055.
    • (1989) Proc. Natl. Acad. Sci. U. S.A. , vol.86 , pp. 2051-2055
    • Radolf, J.D.1    Norgard, M.V.2    Schulz, W.W.3
  • 79
    • 0014382844 scopus 로고
    • Fine structure of the mesosome and nucleoid in frozen-etched bacillus subtilis
    • Remsen C.C. Fine structure of the mesosome and nucleoid in frozen-etched bacillus subtilis. Arch. Mikrobiol. 1968, 61:40-47.
    • (1968) Arch. Mikrobiol. , vol.61 , pp. 40-47
    • Remsen, C.C.1
  • 80
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
    • Reynolds E.S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biol. 1963, 17:208-212.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 81
    • 1942506926 scopus 로고
    • Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation
    • Sabatini D.D., Bensch K., Barrnett R.J. Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. J. Cell Biol. 1963, 17:19-58.
    • (1963) J. Cell Biol. , vol.17 , pp. 19-58
    • Sabatini, D.D.1    Bensch, K.2    Barrnett, R.J.3
  • 82
    • 58849121358 scopus 로고    scopus 로고
    • Electron cryomicroscopy of E. Coli reveals filament bundles involved in plasmid DNA segregation
    • Salje J., Zuber B., Löwe J. Electron cryomicroscopy of E. Coli reveals filament bundles involved in plasmid DNA segregation. Science 2008, 323:509-512.
    • (2008) Science , vol.323 , pp. 509-512
    • Salje, J.1    Zuber, B.2    Löwe, J.3
  • 83
    • 33846231053 scopus 로고    scopus 로고
    • Segmentation of thin structures in electron micrographs using orientation fields
    • Sandberg K., Brega M. Segmentation of thin structures in electron micrographs using orientation fields. J. Struct. Biol. 2007, 157:403-415.
    • (2007) J. Struct. Biol. , vol.157 , pp. 403-415
    • Sandberg, K.1    Brega, M.2
  • 84
    • 35148839574 scopus 로고    scopus 로고
    • Correlative microscopy: Bridging the gap between fluorescence light microscopy and cryo-electron tomography
    • Sartori A., Gatz R., Beck F., Rigort A., Baumeister W., Plitzko J.M. Correlative microscopy: Bridging the gap between fluorescence light microscopy and cryo-electron tomography. J. Struct. Biol. 2007, 160:135-145.
    • (2007) J. Struct. Biol. , vol.160 , pp. 135-145
    • Sartori, A.1    Gatz, R.2    Beck, F.3    Rigort, A.4    Baumeister, W.5    Plitzko, J.M.6
  • 85
    • 34548472879 scopus 로고    scopus 로고
    • Cryo-fluorescence microscopy facilitates correlations between light and cryo-electron microscopy and reduces the rate of photobleaching
    • Schwartz C.L., Sarbash V.I., Ataullakhanov F.I., McIntosh J.R., Nicastro D. Cryo-fluorescence microscopy facilitates correlations between light and cryo-electron microscopy and reduces the rate of photobleaching. J. Microsc. 2007, 227:98-109.
    • (2007) J. Microsc. , vol.227 , pp. 98-109
    • Schwartz, C.L.1    Sarbash, V.I.2    Ataullakhanov, F.I.3    McIntosh, J.R.4    Nicastro, D.5
  • 86
    • 33750512775 scopus 로고    scopus 로고
    • Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography
    • Seybert A., Herrmann R., Frangakis A. Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography. J. Struct. Biol. 2006, 156:342-354.
    • (2006) J. Struct. Biol. , vol.156 , pp. 342-354
    • Seybert, A.1    Herrmann, R.2    Frangakis, A.3
  • 87
    • 0036618137 scopus 로고    scopus 로고
    • Electron microscopic studies of three gliding mycoplasmas, Mycoplasma mobile, M. Pneumoniae, and M. Gallisepticum, by using the freeze-substitution technique
    • Shimizu T., Miyata M. Electron microscopic studies of three gliding mycoplasmas, Mycoplasma mobile, M. Pneumoniae, and M. Gallisepticum, by using the freeze-substitution technique. Curr. Microbiol. 2002, 44:431-434.
    • (2002) Curr. Microbiol. , vol.44 , pp. 431-434
    • Shimizu, T.1    Miyata, M.2
  • 88
    • 0024465753 scopus 로고
    • Quantitative aspects of immunogold labeling in embedded and in nonembedded sections
    • Slot J.W., Posthuma G., Chang L.Y., Crapo J.D., Geuze H.J. Quantitative aspects of immunogold labeling in embedded and in nonembedded sections. Am. J. Anat. 1989, 185:271-281.
    • (1989) Am. J. Anat. , vol.185 , pp. 271-281
    • Slot, J.W.1    Posthuma, G.2    Chang, L.Y.3    Crapo, J.D.4    Geuze, H.J.5
  • 89
    • 18544368222 scopus 로고    scopus 로고
    • In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB
    • Sontag C.A., Staley J.T., Erickson H.P. In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB. J. Cell Biol. 2005, 169:233-238.
    • (2005) J. Cell Biol. , vol.169 , pp. 233-238
    • Sontag, C.A.1    Staley, J.T.2    Erickson, H.P.3
  • 90
    • 77957009283 scopus 로고    scopus 로고
    • Slam-freezing, metal-mirror freezing
    • CRC Press, Boca Raton, A. Cavalier, D. Spehner, B.M. Humbel (Eds.)
    • Spehner D., Edelmann L. Slam-freezing, metal-mirror freezing. Handbook of Cryo-Preparation Methods for Electron Microscopy 2009, 18-47. CRC Press, Boca Raton. A. Cavalier, D. Spehner, B.M. Humbel (Eds.).
    • (2009) Handbook of Cryo-Preparation Methods for Electron Microscopy , pp. 18-47
    • Spehner, D.1    Edelmann, L.2
  • 91
    • 0024853192 scopus 로고
    • Labeling properties of sucrose-infiltrated cryosections
    • Stierhof Y.D., Schwarz H. Labeling properties of sucrose-infiltrated cryosections. Scanning Microsc. Suppl. 1989, 3:35-46.
    • (1989) Scanning Microsc. Suppl. , vol.3 , pp. 35-46
    • Stierhof, Y.D.1    Schwarz, H.2
  • 92
    • 0019362246 scopus 로고
    • Single bacteriorhodopsin molecules revealed on both surfaces of freeze-dried and heavy metal-decorated purple membranes
    • Studer D., Moor H., Gross H. Single bacteriorhodopsin molecules revealed on both surfaces of freeze-dried and heavy metal-decorated purple membranes. J. Cell Biol. 1981, 90:153-159.
    • (1981) J. Cell Biol. , vol.90 , pp. 153-159
    • Studer, D.1    Moor, H.2    Gross, H.3
  • 97
    • 0015620349 scopus 로고
    • A technique for ultracryotomy of cell suspensions and tissues
    • Tokuyasu K.T. A technique for ultracryotomy of cell suspensions and tissues. J. Cell Biol. 1973, 57:551-565.
    • (1973) J. Cell Biol. , vol.57 , pp. 551-565
    • Tokuyasu, K.T.1
  • 99
    • 69249090017 scopus 로고    scopus 로고
    • High-pressure freezing LEICA EMPACT
    • CRC Press, Boca Raton, A. Cavalier, D. Spehner, B.M. Humbel (Eds.)
    • Vanhecke D., Studer D. High-pressure freezing LEICA EMPACT. Handbook of Cryo-Preparation Methods for Electron Microscopy 2009, 129-156. CRC Press, Boca Raton. A. Cavalier, D. Spehner, B.M. Humbel (Eds.).
    • (2009) Handbook of Cryo-Preparation Methods for Electron Microscopy , pp. 129-156
    • Vanhecke, D.1    Studer, D.2
  • 101
    • 70350151669 scopus 로고    scopus 로고
    • Cell division ring, a new cell division protein and vertical inheritance of a bacterial organelle in anammox planctomycetes
    • van Niftrik L., et al. Cell division ring, a new cell division protein and vertical inheritance of a bacterial organelle in anammox planctomycetes. Mol. Microbiol. 2009, 73:1009-1019.
    • (2009) Mol. Microbiol. , vol.73 , pp. 1009-1019
    • van Niftrik, L.1
  • 102
    • 42649111676 scopus 로고    scopus 로고
    • Moving EM: The rapid transfer system as a new tool for correlative light and electron microscopy and high throughput for high-pressure freezing
    • Verkade P. Moving EM: The rapid transfer system as a new tool for correlative light and electron microscopy and high throughput for high-pressure freezing. J. Microsc. 2008, 230:317-328.
    • (2008) J. Microsc. , vol.230 , pp. 317-328
    • Verkade, P.1
  • 104
    • 32544442151 scopus 로고    scopus 로고
    • Observations on the behavior of vitreous ice at ~ 82 and ~ 12K
    • Wright E.R., Iancu C.V., Tivol W.F., Jensen G.J. Observations on the behavior of vitreous ice at ~ 82 and ~ 12K. J. Struct. Biol. 2006, 153:241-252.
    • (2006) J. Struct. Biol. , vol.153 , pp. 241-252
    • Wright, E.R.1    Iancu, C.V.2    Tivol, W.F.3    Jensen, G.J.4
  • 105
    • 33845319257 scopus 로고    scopus 로고
    • UCSF tomography: an integrated software suite for real-time electron microscopic tomographic data collection, alignment, and reconstruction
    • Zheng S.Q., Keszthelyi B., Branlund E., Lyle J.M., Braunfeld M.B., Sedat J.W., Agard D.A. UCSF tomography: an integrated software suite for real-time electron microscopic tomographic data collection, alignment, and reconstruction. J. Struct. Biol. 2007, 157:138-147.
    • (2007) J. Struct. Biol. , vol.157 , pp. 138-147
    • Zheng, S.Q.1    Keszthelyi, B.2    Branlund, E.3    Lyle, J.M.4    Braunfeld, M.B.5    Sedat, J.W.6    Agard, D.A.7


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