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Volumn 62, Issue 1, 2013, Pages 95-107

3D imaging and quantitative analysis of small solubilized membrane proteins and their complexes by transmission electron microscopy

Author keywords

3D electron microscopy; Detergent belt; Membrane protein complex; Negative staining; Rhodopsin transducin complex; Scanning transmission electron microscopy

Indexed keywords

AQUAPORIN; DETERGENT; MEMBRANE PROTEIN; RHODOPSIN; TRANSDUCIN;

EID: 84876703803     PISSN: 00220744     EISSN: 14779986     Source Type: Journal    
DOI: 10.1093/jmicro/dfs091     Document Type: Review
Times cited : (20)

References (66)
  • 2
    • 41149127245 scopus 로고    scopus 로고
    • Vertebrate membrane proteins: Structure, function, and insights from biophysical approaches
    • Muller D J, Wu N, and Palczewski K (2008) Vertebrate membrane proteins: structure, function, and insights from biophysical approaches. Pharmacol. Rev. 60: 43-78.
    • (2008) Pharmacol. Rev. , vol.60 , pp. 43-78
    • Muller, D.J.1    Wu, N.2    Palczewski, K.3
  • 5
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S and Henderson R (2000) Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406: 653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 6
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A, Fujiyoshi Y, and Unwin N (2003) Structure and gating mechanism of the acetylcholine receptor pore. Nature 423: 949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 7
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin N (2005) Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346: 967-989.
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 8
    • 84865696393 scopus 로고    scopus 로고
    • Gating movement of acetylcholine receptor caught by plunge-freezing
    • Unwin N and Fujiyoshi Y (2012) Gating movement of acetylcholine receptor caught by plunge-freezing. J. Mol. Biol. 422: 617-634.
    • (2012) J. Mol. Biol. , vol.422 , pp. 617-634
    • Unwin, N.1    Fujiyoshi, Y.2
  • 9
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E, Wolf S G, and Downing K H (1998) Structure of the alpha beta 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
  • 14
    • 79955032171 scopus 로고    scopus 로고
    • Atomic resolution cryo electron microscopy of macromolecular complexes
    • Zhou Z H (2011) Atomic resolution cryo electron microscopy of macromolecular complexes. Adv. Protein Chem. Struct. Biol. 82: 1-35.
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.82 , pp. 1-35
    • Zhou, Z.H.1
  • 16
    • 0034160037 scopus 로고    scopus 로고
    • Correction of high-resolution data for curvature of the Ewald sphere
    • DeRosier D J (2000) Correction of high-resolution data for curvature of the Ewald sphere. Ultramicroscopy 81: 83-98.
    • (2000) Ultramicroscopy , vol.81 , pp. 83-98
    • Derosier, D.J.1
  • 17
    • 33845666839 scopus 로고    scopus 로고
    • Biological scanning transmission electron microscopy: Imaging and single molecule mass determination
    • Müller S A and Engel A (2006) Biological scanning transmission electron microscopy: imaging and single molecule mass determination. Chimia 60: 749-753.
    • (2006) Chimia , vol.60 , pp. 749-753
    • Müller, S.A.1    Engel, A.2
  • 18
    • 0026499357 scopus 로고
    • Has negative staining still a place in biomacromolecular electron microscopy?
    • Bremer A, Henn C, Engel A, Baumeister W, and Aebi U (1992) Has negative staining still a place in biomacromolecular electron microscopy? Ultramicroscopy 46: 85-111.
    • (1992) Ultramicroscopy , vol.46 , pp. 85-111
    • Bremer, A.1    Henn, C.2    Engel, A.3    Baumeister, W.4    Aebi, U.5
  • 19
    • 29444439322 scopus 로고    scopus 로고
    • Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques
    • Cheng Y, Wolf E, Larvie M, Zak O, Aisen P, Grigorieff N, Harrison SC, and Walz T (2006) Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques. J. Mol. Biol. 355: 1048-1065.
    • (2006) J. Mol. Biol. , vol.355 , pp. 1048-1065
    • Cheng, Y.1    Wolf, E.2    Larvie, M.3    Zak, O.4    Aisen, P.5    Grigorieff, N.6    Harrison, S.C.7    Walz, T.8
  • 20
    • 78649808726 scopus 로고    scopus 로고
    • Negative staining and cryo-negative staining of macromolecules and viruses for TEM
    • De Carlo S and Harris J R (2011) Negative staining and cryo-negative staining of macromolecules and viruses for TEM. Micron 42: 117-131.
    • (2011) Micron , vol.42 , pp. 117-131
    • De Carlo, S.1    Harris, J.R.2
  • 22
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris
    • Karlsson M, Fotiadis D, Sjovall S, Johansson I, Hedfalk K, Engel A, and Kjellbom P (2003) Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris. FEBS Lett. 537: 68-72.
    • (2003) FEBS Lett. , vol.537 , pp. 68-72
    • Karlsson, M.1    Fotiadis, D.2    Sjovall, S.3    Johansson, I.4    Hedfalk, K.5    Engel, A.6    Kjellbom, P.7
  • 23
    • 35148874303 scopus 로고    scopus 로고
    • Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer: Implications for in vitro studies of amphipol-stabilized membrane proteins
    • Zoonens M, Giusti F, Zito F, and Popot J L (2007) Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer: implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry 46: 10392-10404.
    • (2007) Biochemistry , vol.46 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.L.4
  • 24
    • 0029945635 scopus 로고    scopus 로고
    • Semper: Distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system
    • Saxton W O (1996) Semper: distortion compensation, selective averaging, 3-D reconstruction, and transfer function correction in a highly programmable system. J. Struct. Biol. 116: 230-236.
    • (1996) J. Struct. Biol. , vol.116 , pp. 230-236
    • Saxton, W.O.1
  • 25
    • 33646784015 scopus 로고    scopus 로고
    • CTF determination and correction in electron cryotomography
    • Fernandez J J, Li S, and Crowther R A (2006) CTF determination and correction in electron cryotomography. Ultramicroscopy 106: 587-596.
    • (2006) Ultramicroscopy , vol.106 , pp. 587-596
    • Fernandez, J.J.1    Li, S.2    Crowther, R.A.3
  • 27
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, and Frank J (1987) Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 146: 113-136.
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 29
    • 0016068855 scopus 로고
    • A comparison of calculated images by six modes of transmission electron microscopy
    • Engel A, Wiggins J W, and Woodruff D C (1974) A comparison of calculated images by six modes of transmission electron microscopy. J. Appl. Phys. 45: 2739-2747.
    • (1974) J. Appl. Phys. , vol.45 , pp. 2739-2747
    • Engel, A.1    Wiggins, J.W.2    Woodruff, D.C.3
  • 30
    • 77950283360 scopus 로고    scopus 로고
    • Atom-by-atom structural and chemical analysis by annular dark-field electron microscopy
    • Krivanek O (2010) Atom-by-atom structural and chemical analysis by annular dark-field electron microscopy. Nature 464: 571.
    • (2010) Nature , vol.464 , pp. 571
    • Krivanek, O.1
  • 31
    • 0018197443 scopus 로고
    • Molecular weight determination by scanning transmission electron microscopy
    • Engel A (1978) Molecular weight determination by scanning transmission electron microscopy. Ultramicroscopy 3: 273-281.
    • (1978) Ultramicroscopy , vol.3 , pp. 273-281
    • Engel, A.1
  • 32
    • 0022526226 scopus 로고
    • Mass mapping with the scanning transmission electron microscope
    • Wall J S and Hainfeld J F (1986) Mass mapping with the scanning transmission electron microscope. Annu. Rev. Biophys. Biophys. Chem. 15: 355-376.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 355-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 33
    • 58749087507 scopus 로고    scopus 로고
    • MASDET-A fast and user-friendly multiplatform software for mass determination by dark-field electron microscopy
    • Krzyzanek V, Muller S A, Engel A, and Reichelt R (2009) MASDET-A fast and user-friendly multiplatform software for mass determination by dark-field electron microscopy. J. Struct. Biol. 165: 78-87.
    • (2009) J. Struct. Biol. , vol.165 , pp. 78-87
    • Krzyzanek, V.1    Muller, S.A.2    Engel, A.3    Reichelt, R.4
  • 34
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • Müller S A, Goldie K N, Buerki R, Haering R, and Engel A (1992) Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy 46: 317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Buerki, R.3    Haering, R.4    Engel, A.5
  • 35
    • 0031855721 scopus 로고    scopus 로고
    • Mass measurement in the scanning transmission electron microscope: A powerful tool for studying membrane proteins
    • Müller S A and Engel A (1998) Mass measurement in the scanning transmission electron microscope: a powerful tool for studying membrane proteins. J. Struct. Biol. 121: 219-230.
    • (1998) J. Struct. Biol. , vol.121 , pp. 219-230
    • Müller, S.A.1    Engel, A.2
  • 36
    • 0028275784 scopus 로고
    • The threedimensional structure of human erythrocyte aquaporin CHIP
    • Walz T, Smith B L, Agre P, and Engel A (1994) The threedimensional structure of human erythrocyte aquaporin CHIP. EMBO J. 13: 2985-2993.
    • (1994) EMBO J. , vol.13 , pp. 2985-2993
    • Walz, T.1    Smith, B.L.2    Agre, P.3    Engel, A.4
  • 37
    • 0025922827 scopus 로고
    • Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • Smith B L and Agre P (1991) Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266: 6407-6415.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 40
    • 0036427905 scopus 로고    scopus 로고
    • Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles
    • De Carlo S, El-Bez C, Alvarez-Rua C, Borge J, and Dubochet J (2002) Cryo-negative staining reduces electron-beam sensitivity of vitrified biological particles. J. Struct. Biol. 138: 216-226.
    • (2002) J. Struct. Biol. , vol.138 , pp. 216-226
    • De Carlo, S.1    El-Bez, C.2    Alvarez-Rua, C.3    Borge, J.4    Dubochet, J.5
  • 41
    • 48749121595 scopus 로고    scopus 로고
    • High-resolution singleparticle 3D analysis on GroEL prepared by cryo-negative staining
    • De Carlo S, Boisset N, and Hoenger A (2008) High-resolution singleparticle 3D analysis on GroEL prepared by cryo-negative staining. Micron 39: 934-943.
    • (2008) Micron , vol.39 , pp. 934-943
    • De Carlo, S.1    Boisset, N.2    Hoenger, A.3
  • 42
    • 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
  • 44
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski K (2006) G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75: 743-767.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 45
    • 84855845956 scopus 로고    scopus 로고
    • Chemistry and biology of vision
    • Palczewski K (2012) Chemistry and biology of vision. J. Biol. Chem. 287: 1612-1619.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1612-1619
    • Palczewski, K.1
  • 47
    • 39149104024 scopus 로고    scopus 로고
    • GPCR monomers and oligomers: It takes all kinds
    • Gurevich V V and Gurevich E V (2008) GPCR monomers and oligomers: it takes all kinds. Trends Neurosci. 31: 74-81.
    • (2008) Trends Neurosci. , vol.31 , pp. 74-81
    • Gurevich, V.V.1    Gurevich, E.V.2
  • 48
    • 79957516738 scopus 로고    scopus 로고
    • GPCR oligomers in pharmacology and signaling
    • Gonzalez-Maeso J (2011) GPCR oligomers in pharmacology and signaling. Mol. Brain 4: 20.
    • (2011) Mol. Brain , vol.4 , pp. 20
    • Gonzalez-Maeso, J.1
  • 50
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - Powerful tools in modern electron microscopy
    • Ohi M, Li Y, Cheng Y, and Walz T (2004) Negative staining and image classification - powerful tools in modern electron microscopy. Biol. Proced. Online 6: 23-34.
    • (2004) Biol. Proced. Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 51
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire M, Champeil P, and Moller J V (2000) Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta 1508: 86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 52
    • 0016690558 scopus 로고
    • The size and detergent binding of membrane proteins
    • Clarke S (1975) The size and detergent binding of membrane proteins. J. Biol. Chem. 250: 5459-5469.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5459-5469
    • Clarke, S.1
  • 53
    • 0034607357 scopus 로고    scopus 로고
    • Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle
    • Lustig A, Engel A, Tsiotis G, Landau E M, and Baschong W (2000) Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or Nycodenz-adjusted density of the hydrated detergent micelle. Biochimica et Biophysica Acta 1464: 199-206.
    • (2000) Biochimica et Biophysica Acta , vol.1464 , pp. 199-206
    • Lustig, A.1    Engel, A.2    Tsiotis, G.3    Landau, E.M.4    Baschong, W.5
  • 54
    • 55649115081 scopus 로고    scopus 로고
    • Determination of the molecular mass and dimensions of membrane proteins by size exclusion chromatography
    • Kunji E R, Harding M, Butler P J, and Akamine P (2008) Determination of the molecular mass and dimensions of membrane proteins by size exclusion chromatography. Methods 46: 62-72.
    • (2008) Methods , vol.46 , pp. 62-72
    • Kunji, E.R.1    Harding, M.2    Butler, P.J.3    Akamine, P.4
  • 55
    • 33646163904 scopus 로고    scopus 로고
    • A novel method for detergent concentration determination
    • Kaufmann T C, Engel A, and Remigy H W (2006) A novel method for detergent concentration determination. Biophys. J. 90: 310-317.
    • (2006) Biophys. J. , vol.90 , pp. 310-317
    • Kaufmann, T.C.1    Engel, A.2    Remigy, H.W.3
  • 56
    • 0035239217 scopus 로고    scopus 로고
    • Structure and mass analysis by scanning transmission electron microscopy
    • Müller S A and Engel A (2000) Structure and mass analysis by scanning transmission electron microscopy. Micron 32: 21-31.
    • (2000) Micron , vol.32 , pp. 21-31
    • Müller, S.A.1    Engel, A.2
  • 61
    • 81255210901 scopus 로고    scopus 로고
    • Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1
    • Althoff T, Mills D J, Popot J L, and Kuhlbrandt W (2011) Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J. 30: 4652-4664.
    • (2011) EMBO J. , vol.30 , pp. 4652-4664
    • Althoff, T.1    Mills, D.J.2    Popot, J.L.3    Kuhlbrandt, W.4
  • 62
    • 80055073153 scopus 로고    scopus 로고
    • Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy
    • Cvetkov T L, Huynh K W, Cohen M R, and Moiseenkova-Bell V Y (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J. Biol. Chem. 286: 38168-38176.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38168-38176
    • Cvetkov, T.L.1    Huynh, K.W.2    Cohen, M.R.3    Moiseenkova-Bell, V.Y.4
  • 64
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P, Radermacher M, and Frank J (1992) Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 40: 33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 65
    • 0027106192 scopus 로고
    • Alignment, classification, and three-dimensional reconstruction of single particles embedded in ice
    • Frank J, Penczek P, and Liu W (1992) Alignment, classification, and three-dimensional reconstruction of single particles embedded in ice. Scanning Microsc. Suppl. 6: 11-20.
    • (1992) Scanning Microsc. Suppl. , vol.6 , pp. 11-20
    • Frank, J.1    Penczek, P.2    Liu, W.3
  • 66
    • 0021645447 scopus 로고
    • Multivariate statistical classification of noisy images (randomly oriented biological macromolecules)
    • van Heel M (1984) Multivariate statistical classification of noisy images (randomly oriented biological macromolecules). Ultramicroscopy 13: 165-183.
    • (1984) Ultramicroscopy , vol.13 , pp. 165-183
    • Van Heel, M.1


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