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Volumn 48, Issue 5, 1999, Pages 653-658

Trehalose embedding technique for high-resolution electron crystallography: Application to structural study on bacteriorhoposin

Author keywords

Diffraction pattern; Electron crystallography; Electron microscopy; Glucose embedding; Hydration; Trehalose embedding

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0032695274     PISSN: 00220744     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jmicro.a023731     Document Type: Article
Times cited : (52)

References (33)
  • 2
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin P N T and Henderson R (1975) Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94: 425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 3
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R and Unwin P N T (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature 257: 28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 4
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin J M, Ceska T A, Zemlin F, Beckmann E, and Downing K H (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. 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    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 6
    • 0026061928 scopus 로고
    • High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media
    • Wang D N and Kühlbrandt W (1991) High-resolution electron crystallography of light-harvesting chlorophyll a/b-protein complex in three different media. J. Mol. Biol. 217: 691-699.
    • (1991) J. Mol. Biol. , vol.217 , pp. 691-699
    • Wang, D.N.1    Kühlbrandt, W.2
  • 7
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt W, Wang D N, and Fujiyoshi Y (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367: 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 8
    • 0028856299 scopus 로고
    • Preservation of 2-D crystals of tubulin for electron crystallography
    • Nogales E, Wolf S G, Zhang S X, and Downing K H (1995) Preservation of 2-D crystals of tubulin for electron crystallography. J. Struct. Biol. 115: 199-208.
    • (1995) J. Struct. Biol. , vol.115 , pp. 199-208
    • Nogales, E.1    Wolf, S.G.2    Zhang, S.X.3    Downing, K.H.4
  • 9
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf S G, and Downing K H (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature 391: 199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 10
    • 0025602922 scopus 로고
    • Frozen and alive
    • December
    • Storey K B and Storey J M (1990) Frozen and alive. Sci. Am., December: 92-97.
    • (1990) Sci. Am. , pp. 92-97
    • Storey, K.B.1    Storey, J.M.2
  • 11
    • 0001478785 scopus 로고
    • The crystal structure of α,α-trehalose dihydrate from three independent X-ray determinations
    • Brown G M (1972) The crystal structure of α,α-trehalose dihydrate from three independent X-ray determinations. Acta Cryst. B 28: 3145-3158.
    • (1972) Acta Cryst. B , vol.28 , pp. 3145-3158
    • Brown, G.M.1
  • 12
    • 0023653939 scopus 로고
    • Stabilization of dry phospholipid bilayers and proteins by sugars
    • Crowe J H, Crowe L M, Carpenter J F, and Wistrom C A (1987) Stabilization of dry phospholipid bilayers and proteins by sugars. Biochem. J. 242: 1986-1987.
    • (1987) Biochem. J. , vol.242 , pp. 1986-1987
    • Crowe, J.H.1    Crowe, L.M.2    Carpenter, J.F.3    Wistrom, C.A.4
  • 13
    • 0002509009 scopus 로고
    • Trehalose drying: A novel replacement for freeze-drying
    • September
    • Roser B (1991) Trehalose drying: a novel replacement for freeze-drying. BioPharm, September: 47-53.
    • (1991) BioPharm , pp. 47-53
    • Roser, B.1
  • 14
    • 50749134719 scopus 로고
    • Trehalose, a new approach to premium dried foods
    • July
    • Roser B (1991) Trehalose, a new approach to premium dried foods. Trends Food Sci. Tech., July: 166-169.
    • (1991) Trends Food Sci. Tech. , pp. 166-169
    • Roser, B.1
  • 15
    • 0026941297 scopus 로고
    • Hydration of oligosaccharides: Anomalous hydration ability of trehalose
    • Kawai H, Sakurai M, lnoue Y, Chujo R, and Kobayashi S (1992) Hydration of oligosaccharides: anomalous hydration ability of trehalose. Cryobiology 29: 599-606.
    • (1992) Cryobiology , vol.29 , pp. 599-606
    • Kawai, H.1    Sakurai, M.2    Inoue, Y.3    Chujo, R.4    Kobayashi, S.5
  • 16
    • 0345602462 scopus 로고
    • Trehalose mimics a role of water in dryness
    • Hirasawa K (1993) Trehalose mimics a role of water in dryness. Nippon Kesshou Gakkaishi 35: 3-34.
    • (1993) Nippon Kesshou Gakkaishi , vol.35 , pp. 3-34
    • Hirasawa, K.1
  • 18
    • 0028487168 scopus 로고
    • Is vitrification sufficient to preserve liposomes during freeze-drying?
    • Crowe J H, Leslie S B, and Crowe L M (1994) Is vitrification sufficient to preserve liposomes during freeze-drying? Cryobiology 31: 355-366.
    • (1994) Cryobiology , vol.31 , pp. 355-366
    • Crowe, J.H.1    Leslie, S.B.2    Crowe, L.M.3
  • 19
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe L M, Reid D S, and Crowe J H (1996) Is trehalose special for preserving dry biomaterials? Biophys. J. 71: 2087-2093.
    • (1996) Biophys. J. , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2    Crowe, J.H.3
  • 20
    • 17144427046 scopus 로고    scopus 로고
    • Negative stains containing trehalose: Application to tubular and filamentous structures
    • Harris J R, Gerber M, Gebauer W, Wernicke W, and Markl J (1996) Negative stains containing trehalose: application to tubular and filamentous structures. JMSA 2: 43-52.
    • (1996) JMSA , vol.2 , pp. 43-52
    • Harris, J.R.1    Gerber, M.2    Gebauer, W.3    Wernicke, W.4    Markl, J.5
  • 21
    • 0025297219 scopus 로고
    • Structure of PhoE porin in projection at 3.5Å resolution
    • Jap B K, Downing K H, and Walian P J (1990) Structure of PhoE porin in projection at 3.5Å resolution. J. Struct. Biol. 103:57-63.
    • (1990) J. Struct. Biol. , vol.103 , pp. 57-63
    • Jap, B.K.1    Downing, K.H.2    Walian, P.J.3
  • 22
    • 0025806797 scopus 로고
    • Structural architecture of an outer membrane channel as determined by electron crystallography
    • Jap B K, Walian P J, and 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
  • 26
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D and Stoeckenius W (1974) Isolation of the cell membrane of halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31: 667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 27
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J and Henderson R (1984) Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy 14: 319-336.
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.1    Henderson, R.2
  • 28
    • 0027561407 scopus 로고
    • Cryo-crinkling: What happens to carbon films on copper grids at low temperature
    • Booy F P and Pawley J B (1993) Cryo-crinkling: what happens to carbon films on copper grids at low temperature. Ultramicroscopy 48: 273-280.
    • (1993) Ultramicroscopy , vol.48 , pp. 273-280
    • Booy, F.P.1    Pawley, J.B.2
  • 30
    • 0026053859 scopus 로고
    • Interfacial energies and surface-tension forces involved in the preparation of thin, flat crystals of biological macromolecules for high-resolution electron microscopy
    • Glaeser R M, Zilker A, Radermacher M, Gaub H E, Hartmann T, and Baumeister W (1991) Interfacial energies and surface-tension forces involved in the preparation of thin, flat crystals of biological macromolecules for high-resolution electron microscopy. J. Microsc. 161: 21-45.
    • (1991) J. Microsc. , vol.161 , pp. 21-45
    • Glaeser, R.M.1    Zilker, A.2    Radermacher, M.3    Gaub, H.E.4    Hartmann, T.5    Baumeister, W.6
  • 32
    • 0027540566 scopus 로고
    • Applications of slow-scan CCD cameras in transmission electron microscopy
    • Krivanek O L and Mooney P E (1993) Applications of slow-scan CCD cameras in transmission electron microscopy. Ultramicroscopy 49: 95-108.
    • (1993) Ultramicroscopy , vol.49 , pp. 95-108
    • Krivanek, O.L.1    Mooney, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.