메뉴 건너뛰기




Volumn 62, Issue 1, 2013, Pages 43-50

Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice

Author keywords

Apoferritin; Beta galactosidase; CryoEM; Perfect images; Single particles; Tilt pairs

Indexed keywords

APOFERRITIN; BETA GALACTOSIDASE; ICE;

EID: 84876978430     PISSN: 00220744     EISSN: 14779986     Source Type: Journal    
DOI: 10.1093/jmicro/dfs094     Document Type: Review
Times cited : (35)

References (22)
  • 1
    • 0021786909 scopus 로고
    • Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals
    • Henderson R and Glaeser R M (1985) Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals. Ultramicroscopy 16: 139-150.
    • (1985) Ultramicroscopy , vol.16 , pp. 139-150
    • Henderson, R.1    Glaeser, R.M.2
  • 2
    • 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
  • 3
    • 67650544797 scopus 로고    scopus 로고
    • Detective quantum efficiency of electron area detectors in electron microscopy
    • McMullan G, Chen S, Henderson R, and Faruqi A R (2009) Detective quantum efficiency of electron area detectors in electron microscopy. Ultramicroscopy 109: 1126-1143.
    • (2009) Ultramicroscopy , vol.109 , pp. 1126-1143
    • McMullan, G.1    Chen, S.2    Henderson, R.3    Faruqi, A.R.4
  • 4
    • 78349286395 scopus 로고    scopus 로고
    • Images of paraffin monolayer crystals with perfect contrast: Minimization of beam-induced specimen motion
    • Glaeser R M, McMullan G, Faruqi A R, and Henderson R (2011) Images of paraffin monolayer crystals with perfect contrast: minimization of beam-induced specimen motion. Ultramicroscopy 111: 90-100.
    • (2011) Ultramicroscopy , vol.111 , pp. 90-100
    • Glaeser, R.M.1    McMullan, G.2    Faruqi, A.R.3    Henderson, R.4
  • 5
    • 0030174932 scopus 로고    scopus 로고
    • Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures
    • Stark H, Zemlin F, and Boettcher C (1996) Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures. Ultramicroscopy 63: 75-79.
    • (1996) Ultramicroscopy , vol.63 , pp. 75-79
    • Stark, H.1    Zemlin, F.2    Boettcher, C.3
  • 9
    • 32544442151 scopus 로고    scopus 로고
    • Observations on the behavior of vitreous ice at ∼82 and ∼12 K
    • Wright E R, Lancu C V, Tivol W F, and Jensen G J (2006) Observations on the behavior of vitreous ice at ∼82 and ∼12 K. J. Struct. Biol. 153: 241-252.
    • (2006) J. Struct. Biol. , vol.153 , pp. 241-252
    • Wright, E.R.1    Lancu, C.V.2    Tivol, W.F.3    Jensen, G.J.4
  • 10
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in singleparticle electron cryomicroscopy
    • Rosenthal P B and Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in singleparticle electron cryomicroscopy. J. Mol. Biol. 333: 721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 11
    • 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
  • 12
    • 0030922840 scopus 로고    scopus 로고
    • Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin
    • Granier T, Gallois B, Dautant A, d'Estaintot B L, and Precigoux G (1997) Comparison of the structures of the cubic and tetragonal forms of horse-spleen apoferritin. Acta Cryst. D. 53: 580-587.
    • (1997) Acta Cryst. D. , vol.53 , pp. 580-587
    • Granier, T.1    Gallois, B.2    Dautant, A.3    D'Estaintot, B.L.4    Precigoux, G.5
  • 13
    • 76749094569 scopus 로고    scopus 로고
    • The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals
    • Baker L A, Smith E A, Bueler S A, and Rubinstein J L (2010) The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals. J. Struct. Biol. 169: 431-437.
    • (2010) J. Struct. Biol. , vol.169 , pp. 431-437
    • Baker, L.A.1    Smith, E.A.2    Bueler, S.A.3    Rubinstein, J.L.4
  • 16
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Ångstrom cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui W H, and Zhou Z H (2010) 3.3 Ångstrom cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141: 472-482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 17
    • 79955867558 scopus 로고    scopus 로고
    • Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses
    • Yu X K, Ge P, Jiang J S, Atanasov I, and Zhou Z H (2011) Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses. Structure 19: 652-661.
    • (2011) Structure , vol.19 , pp. 652-661
    • Yu, X.K.1    Ge, P.2    Jiang, J.S.3    Atanasov, I.4    Zhou, Z.H.5
  • 21
    • 84879038703 scopus 로고    scopus 로고
    • 420-reducing-dehydrogenase from a methanogenic archaeon by cryo-electron microscopy
    • (in press)
    • 420-reducing-dehydrogenase from a methanogenic archaeon by cryo-electron microscopy. eLIFE (in press).
    • (2013) ELIFE
    • Mills, D.1    Vitt, S.2    Strauss, M.3    Shima, S.4    Vonck, J.5
  • 22
    • 78649261616 scopus 로고    scopus 로고
    • Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli)
    • Dugdale M L, Dymianiw D L, Minhas B K, D'Angelo I, and Huber R E (2010) Role of Met-542 as a guide for the conformational changes of Phe-601 that occur during the reaction of β-galactosidase (Escherichia coli). Biochem. Cell Biol. 88: 861-869.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 861-869
    • Dugdale, M.L.1    Dymianiw, D.L.2    Minhas, B.K.3    D'Angelo, I.4    Huber, R.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.