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Volumn 175, Issue 3, 2011, Pages 253-263

Limiting factors in atomic resolution cryo electron microscopy: No simple tricks

Author keywords

Atomic resolution; Beam tilt; CryoEM; Defocus gradient; Dynamic scattering

Indexed keywords

CRYOELECTRON MICROSCOPY; ELECTRON; ELECTRON BEAM; ELECTRON MICROSCOPY; IMAGE PROCESSING; IMAGE QUALITY; IMAGE RECONSTRUCTION; MAGNETIC FIELD; PRIORITY JOURNAL; REVIEW; TILTING;

EID: 79960907297     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.05.004     Document Type: Review
Times cited : (57)

References (58)
  • 1
    • 28844509495 scopus 로고    scopus 로고
    • A practical method to detect and correct for lens distortion in the TEM
    • Capitani G.C., Oleynikov P., Hovmoller S., Mellini M. A practical method to detect and correct for lens distortion in the TEM. Ultramicroscopy 2006, 106:66-74.
    • (2006) Ultramicroscopy , vol.106 , pp. 66-74
    • Capitani, G.C.1    Oleynikov, P.2    Hovmoller, S.3    Mellini, M.4
  • 3
    • 79952178436 scopus 로고    scopus 로고
    • Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping
    • Cheng L., Sun J., Zhang K., Mou Z., Huang X., Ji G., Sun F., Zhang J., Zhu P. Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping. Proc. Natl. Acad. Sci. USA 2011, 108:1373-1378.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1373-1378
    • Cheng, L.1    Sun, J.2    Zhang, K.3    Mou, Z.4    Huang, X.5    Ji, G.6    Sun, F.7    Zhang, J.8    Zhu, P.9
  • 6
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1971, 261:221-230.
    • (1971) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 7
    • 0034160037 scopus 로고    scopus 로고
    • Correction of high-resolution data for curvature of the Ewald sphere
    • DeRosier D.J. Correction of high-resolution data for curvature of the Ewald sphere. Ultramicroscopy 2000, 81:83-98.
    • (2000) Ultramicroscopy , vol.81 , pp. 83-98
    • DeRosier, D.J.1
  • 8
    • 33749255323 scopus 로고    scopus 로고
    • Short note on parallel illumination in the TEM
    • Eyidi D., Hébert C., Schattschneider P. Short note on parallel illumination in the TEM. Ultramicroscopy 2006, 106:1144-1149.
    • (2006) Ultramicroscopy , vol.106 , pp. 1144-1149
    • Eyidi, D.1    Hébert, C.2    Schattschneider, P.3
  • 9
    • 79959347866 scopus 로고    scopus 로고
    • Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches
    • Ge, P., Zhou, Z.H., 2011. Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches. Proc. Natl. Acad. Sci. 108. doi:10.1073/pnas.1018104108.
    • (2011) Proc. Natl. Acad. Sci. , vol.108
    • Ge, P.1    Zhou, Z.H.2
  • 10
    • 0000520380 scopus 로고
    • High-voltage electron diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical
    • Glaeser R.M., Ceska T.A. High-voltage electron diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical. Acta Crystallogr. A 1989, 45(Pt 9):620-628.
    • (1989) Acta Crystallogr. A , vol.45 , Issue.PART 9 , pp. 620-628
    • Glaeser, R.M.1    Ceska, T.A.2
  • 11
    • 0027724446 scopus 로고
    • High-resolution electron crystallography of protein molecules
    • Glaeser R.M., Downing K.H. High-resolution electron crystallography of protein molecules. Ultramicroscopy 1993, 52:478-486.
    • (1993) Ultramicroscopy , vol.52 , pp. 478-486
    • Glaeser, R.M.1    Downing, K.H.2
  • 13
    • 39149091041 scopus 로고    scopus 로고
    • Preparation of macromolecular complexes for cryo-electron microscopy
    • Grassucci R.A., Taylor D.J., Frank J. Preparation of macromolecular complexes for cryo-electron microscopy. Nat. Protoc. 2007, 2:3239-3246.
    • (2007) Nat. Protoc. , vol.2 , pp. 3239-3246
    • Grassucci, R.A.1    Taylor, D.J.2    Frank, J.3
  • 14
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 2007, 157:117-125.
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 15
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff N., Harrison S.C. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy. Curr. Opin. Struct. Biol. 2011, 21:265-273.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.2
  • 16
    • 0030250542 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff N., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. Ultramicroscopy 1996, 65:101-107.
    • (1996) Ultramicroscopy , vol.65 , pp. 101-107
    • Grigorieff, N.1    Henderson, R.2
  • 17
    • 0018860552 scopus 로고
    • Units and conventions in electron microscopy, for use in ultramicroscopy
    • Hawkes P.W. Units and conventions in electron microscopy, for use in ultramicroscopy. Ultramicroscopy 1980, 5:67-70.
    • (1980) Ultramicroscopy , vol.5 , pp. 67-70
    • Hawkes, P.W.1
  • 18
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson R. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 1995, 28:171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 19
    • 0039507411 scopus 로고
    • Structure of purple membrane from halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5Å resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., Zemlin F. Structure of purple membrane from halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5Å resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 20
    • 0034039202 scopus 로고    scopus 로고
    • Defocus-gradient corrected back-projection
    • Jensen G.J., Kornberg R.D. Defocus-gradient corrected back-projection. Ultramicroscopy 2000, 84:57-64.
    • (2000) Ultramicroscopy , vol.84 , pp. 57-64
    • Jensen, G.J.1    Kornberg, R.D.2
  • 21
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W., Baker M.L., Jakana J., Weigele P.R., King J., Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 2008, 451:1130-1134.
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 22
    • 0026816671 scopus 로고
    • Practical autoalignment of transmission electron microscopes
    • Koster A.J., de Ruijter W.J. Practical autoalignment of transmission electron microscopes. Ultramicroscopy 1992, 40:89-107.
    • (1992) Ultramicroscopy , vol.40 , pp. 89-107
    • Koster, A.J.1    de Ruijter, W.J.2
  • 24
    • 0016962778 scopus 로고
    • Origin of the fringe structure observed in high resolution bright-field electron micrographs of amorphous materials
    • Krakow W., Ast D.G., Goldfarb W., Siegel B.M. Origin of the fringe structure observed in high resolution bright-field electron micrographs of amorphous materials. Philos. Mag. 1976, 33:985-1014.
    • (1976) Philos. Mag. , vol.33 , pp. 985-1014
    • Krakow, W.1    Ast, D.G.2    Goldfarb, W.3    Siegel, B.M.4
  • 25
    • 77957309181 scopus 로고    scopus 로고
    • Correcting for the ewald sphere in high-resolution single-particle reconstructions
    • Leong P.A., Yu X., Zhou Z.H., Jensen G.J. Correcting for the ewald sphere in high-resolution single-particle reconstructions. Methods Enzymol. 2010, 482:369-380.
    • (2010) Methods Enzymol. , vol.482 , pp. 369-380
    • Leong, P.A.1    Yu, X.2    Zhou, Z.H.3    Jensen, G.J.4
  • 26
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 2010, 329:1038-1043.
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 27
    • 79960912692 scopus 로고
    • Electron beam analysis of materials. In: Electron Beam Analysis of Materials. Chapman and Hall Ltd., London
    • Loretto, M.H., 1984. Electron beam analysis of materials. In: Electron Beam Analysis of Materials. Chapman and Hall Ltd., London, pp. 7-11.
    • (1984) , pp. 7-11
    • Loretto, M.H.1
  • 28
    • 40049105503 scopus 로고    scopus 로고
    • De novo backbone trace of GroEL from single particle electron cryomicroscopy
    • Ludtke S.J., Baker M.L., Chen D.H., Song J.L., Chuang D.T., Chiu W. De novo backbone trace of GroEL from single particle electron cryomicroscopy. Structure 2008, 16:441-448.
    • (2008) Structure , vol.16 , pp. 441-448
    • Ludtke, S.J.1    Baker, M.L.2    Chen, D.H.3    Song, J.L.4    Chuang, D.T.5    Chiu, W.6
  • 29
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 2003, 142:334-347.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 30
    • 0035526199 scopus 로고    scopus 로고
    • Sub-Angstrom resolution of atomistic structure below 0.8A
    • O'Keefe M.A., Nelson E.C., Wang Y.C., Thust A. Sub-Angstrom resolution of atomistic structure below 0.8A. Philos. Mag. B 2001, 81:1861-1878.
    • (2001) Philos. Mag. B , vol.81 , pp. 1861-1878
    • O'Keefe, M.A.1    Nelson, E.C.2    Wang, Y.C.3    Thust, A.4
  • 31
    • 0024475524 scopus 로고
    • Magnification calibration and the determination of spherical virus diameters using cryo-microscopy
    • Olson N.H., Baker T.S. Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicroscopy 1989, 30:281-297.
    • (1989) Ultramicroscopy , vol.30 , pp. 281-297
    • Olson, N.H.1    Baker, T.S.2
  • 32
    • 0031171955 scopus 로고    scopus 로고
    • Correction of three-fold astigmatism for ultra-high-resolution TEM
    • Overwijk M.H.F., Bleeker A.J., Thust A. Correction of three-fold astigmatism for ultra-high-resolution TEM. Ultramicroscopy 1997, 67:163-170.
    • (1997) Ultramicroscopy , vol.67 , pp. 163-170
    • Overwijk, M.H.F.1    Bleeker, A.J.2    Thust, A.3
  • 33
    • 44149111560 scopus 로고    scopus 로고
    • Electron cryo-microscopy of biological specimens on conductive titanium-silicon metal glass films
    • Rhinow D., Kuhlbrandt W. Electron cryo-microscopy of biological specimens on conductive titanium-silicon metal glass films. Ultramicroscopy 2008, 108:698-705.
    • (2008) Ultramicroscopy , vol.108 , pp. 698-705
    • Rhinow, D.1    Kuhlbrandt, W.2
  • 34
    • 0021034131 scopus 로고
    • The importance of beam alignment and crystal tilt in high resolution electron microscopy
    • Smith D.J., Saxton W.O., O'Keefe M.A., Wood G.J., Stobbs W.M. The importance of beam alignment and crystal tilt in high resolution electron microscopy. Ultramicroscopy 1983, 11:263-281.
    • (1983) Ultramicroscopy , vol.11 , pp. 263-281
    • Smith, D.J.1    Saxton, W.O.2    O'Keefe, M.A.3    Wood, G.J.4    Stobbs, W.M.5
  • 37
    • 27544470306 scopus 로고    scopus 로고
    • Magnification variations due to illumination curvature and object defocus in transmission electron microscopy
    • van Duinen G., van Heel M., Patwardhan A. Magnification variations due to illumination curvature and object defocus in transmission electron microscopy. Opt. Express 2005, 13:9085-9093.
    • (2005) Opt. Express , vol.13 , pp. 9085-9093
    • van Duinen, G.1    van Heel, M.2    Patwardhan, A.3
  • 38
    • 11244252897 scopus 로고    scopus 로고
    • Full contrast transfer function correction in 3D cryo-EM reconstruction
    • Wan Y., Chiu W., Zhou Z.H. Full contrast transfer function correction in 3D cryo-EM reconstruction. IEEE Proc. ICCCAS 2004, 2004:960-964.
    • (2004) IEEE Proc. ICCCAS , vol.2004 , pp. 960-964
    • Wan, Y.1    Chiu, W.2    Zhou, Z.H.3
  • 39
    • 0023846548 scopus 로고
    • Structure determination and correction for distortions in HREM by crystallographic image processing
    • Wang D., Hovmöller S., Kihlborg L., Sundberg M. Structure determination and correction for distortions in HREM by crystallographic image processing. Ultramicroscopy 1988, 25:303-316.
    • (1988) Ultramicroscopy , vol.25 , pp. 303-316
    • Wang, D.1    Hovmöller, S.2    Kihlborg, L.3    Sundberg, M.4
  • 40
    • 33344463113 scopus 로고    scopus 로고
    • Ewald sphere correction for single-particle electron microscopy
    • Wolf M., DeRosier D.J., Grigorieff N. Ewald sphere correction for single-particle electron microscopy. Ultramicroscopy 2006, 106:376-382.
    • (2006) Ultramicroscopy , vol.106 , pp. 376-382
    • Wolf, M.1    DeRosier, D.J.2    Grigorieff, N.3
  • 42
    • 0035054774 scopus 로고    scopus 로고
    • An accurate analytical approach to electron crystallography
    • Yang Q., Wang Y., Liu Q., Yan X. An accurate analytical approach to electron crystallography. Ultramicroscopy 2001, 87:177-186.
    • (2001) Ultramicroscopy , vol.87 , pp. 177-186
    • Yang, Q.1    Wang, Y.2    Liu, Q.3    Yan, X.4
  • 43
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 2003, 424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 44
    • 43749092377 scopus 로고    scopus 로고
    • 3.88Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu X., Jin L., Zhou Z.H. 3.88Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 2008, 453:415-419.
    • (2008) Nature , vol.453 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 45
    • 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., Ge P., Jiang J., Atanasov I., Zhou Z.H. Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses. Structure 2011, 19:652-661.
    • (2011) Structure , vol.19 , pp. 652-661
    • Yu, X.1    Ge, P.2    Jiang, J.3    Atanasov, I.4    Zhou, Z.H.5
  • 46
    • 37949044568 scopus 로고
    • Aberration correction in a low voltage SEM by a multipole corrector
    • Zach J., Haider M. Aberration correction in a low voltage SEM by a multipole corrector. Nucl. Instr. Methods Phys. Res. A 1995, 363:316-325.
    • (1995) Nucl. Instr. Methods Phys. Res. A , vol.363 , pp. 316-325
    • Zach, J.1    Haider, M.2
  • 47
    • 0018227155 scopus 로고
    • Coma-free alignment of high resolution electron microscopes with the aid of optical diffractograms
    • Zemlin F. Coma-free alignment of high resolution electron microscopes with the aid of optical diffractograms. Ultramicroscopy 1978, 3:49-60.
    • (1978) Ultramicroscopy , vol.3 , pp. 49-60
    • Zemlin, F.1
  • 48
    • 0018365012 scopus 로고
    • A practical procedure for alignment of a high resolution electron microscope
    • Zemlin F. A practical procedure for alignment of a high resolution electron microscope. Ultramicroscopy 1979, 4:241-245.
    • (1979) Ultramicroscopy , vol.4 , pp. 241-245
    • Zemlin, F.1
  • 49
    • 0024698676 scopus 로고
    • Interferometric measurement of axial coma in electron-microscopical images
    • Zemlin F. Interferometric measurement of axial coma in electron-microscopical images. Ultramicroscopy 1989, 30:311-314.
    • (1989) Ultramicroscopy , vol.30 , pp. 311-314
    • Zemlin, F.1
  • 50
    • 0026932437 scopus 로고
    • Desired features of a cryoelectron microscope for the electron crystallography of biological material
    • Zemlin F. Desired features of a cryoelectron microscope for the electron crystallography of biological material. Ultramicroscopy 1992, 46:25-32.
    • (1992) Ultramicroscopy , vol.46 , pp. 25-32
    • Zemlin, F.1
  • 53
    • 77950907290 scopus 로고    scopus 로고
    • Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins
    • Zhang X., Boyce M., Bhattacharya B., Zhang X., Schein S., Roy P., Zhou Z.H. Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins. Proc. Natl. Acad. Sci. USA 2010, 107:6292-6297.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6292-6297
    • Zhang, X.1    Boyce, M.2    Bhattacharya, B.3    Zhang, X.4    Schein, S.5    Roy, P.6    Zhou, Z.H.7
  • 54
    • 77951912692 scopus 로고    scopus 로고
    • 3.3Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X., Jin L., Fang Q., Hui W.H., Zhou Z.H. 3.3Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 2010, 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
  • 55
    • 41949099222 scopus 로고    scopus 로고
    • Towards atomic resolution structural determination by single-particle cryo-electron microscopy
    • Zhou Z.H. Towards atomic resolution structural determination by single-particle cryo-electron microscopy. Curr. Opin. Struct. Biol. 2008, 18:218-228.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 218-228
    • Zhou, Z.H.1
  • 56
    • 79955032171 scopus 로고    scopus 로고
    • Atomic resolution cryo electron microscopy of macromolecular complexes
    • Zhou Z.H. Atomic resolution cryo electron microscopy of macromolecular complexes. Adv. Protein Chem. Struct. Biol. 2011, 82:1-35.
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.82 , pp. 1-35
    • Zhou, Z.H.1
  • 57
    • 0027543395 scopus 로고
    • Prospects for using an IVEM with a FEG for imaging macromolecules towards atomic resolution
    • Zhou Z.H., Chiu W. Prospects for using an IVEM with a FEG for imaging macromolecules towards atomic resolution. Ultramicroscopy 1993, 49:407-416.
    • (1993) Ultramicroscopy , vol.49 , pp. 407-416
    • Zhou, Z.H.1    Chiu, W.2
  • 58
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou Z.H., Hardt S., Wang B., Sherman M.B., Jakana J., Chiu W. CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 1996, 116:216-222.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-222
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6


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