메뉴 건너뛰기




Volumn 20, Issue 11, 2012, Pages 1823-1828

Movies of ice-embedded particles enhance resolution in electron cryo-microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; AUDIOVISUAL EQUIPMENT; CRYOELECTRON MICROSCOPY; IMAGE ENHANCEMENT; PRIORITY JOURNAL; THREE DIMENSIONAL IMAGING;

EID: 84868573207     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.08.026     Document Type: Article
Times cited : (227)

References (40)
  • 1
    • 76749094569 scopus 로고    scopus 로고
    • The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals
    • L.A. Baker, E.A. Smith, S.A. Bueler, and J.L. Rubinstein The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals J. Struct. Biol. 169 2010 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
  • 2
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • B. Böttcher, S.A. Wynne, and R.A. Crowther Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy Nature 386 1997 88 91
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 4
    • 0023206468 scopus 로고
    • Use of spot-scan procedure for recording low-dose micrographs of beam-sensitive specimens
    • P. Bullough, and R. Henderson Use of spot-scan procedure for recording low-dose micrographs of beam-sensitive specimens Ultramicroscopy 21 1987 223 229
    • (1987) Ultramicroscopy , vol.21 , pp. 223-229
    • Bullough, P.1    Henderson, R.2
  • 5
    • 33846390605 scopus 로고    scopus 로고
    • Design of a microfabricated, two-electrode phase-contrast element suitable for electron microscopy
    • R. Cambie, K.H. Downing, D. Typke, R.M. Glaeser, and J. Jin Design of a microfabricated, two-electrode phase-contrast element suitable for electron microscopy Ultramicroscopy 107 2007 329 339
    • (2007) Ultramicroscopy , vol.107 , pp. 329-339
    • Cambie, R.1    Downing, K.H.2    Typke, D.3    Glaeser, R.M.4    Jin, J.5
  • 8
    • 0034903709 scopus 로고    scopus 로고
    • Transmission electron microscopy with Zernike phase plate
    • R. Danev, and K. Nagayama Transmission electron microscopy with Zernike phase plate Ultramicroscopy 88 2001 243 252
    • (2001) Ultramicroscopy , vol.88 , pp. 243-252
    • Danev, R.1    Nagayama, K.2
  • 9
    • 0032126299 scopus 로고    scopus 로고
    • Perforated support foils with pre-defined hole size, shape and arrangement
    • E. Ermantraut, K. Wohlfart, and W. Tichelaar Perforated support foils with pre-defined hole size, shape and arrangement Ultramicroscopy 74 1998 75 81
    • (1998) Ultramicroscopy , vol.74 , pp. 75-81
    • Ermantraut, E.1    Wohlfart, K.2    Tichelaar, W.3
  • 10
    • 0033377941 scopus 로고    scopus 로고
    • Review: Electron crystallography: Present excitement, a nod to the past, anticipating the future
    • R.M. Glaeser Review: electron crystallography: present excitement, a nod to the past, anticipating the future J. Struct. Biol. 128 1999 3 14
    • (1999) J. Struct. Biol. , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 12
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • N. Grigorieff Resolution measurement in structures derived from single particles Acta Crystallogr. D Biol. Crystallogr. 56 2000 1270 1277
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1270-1277
    • Grigorieff, N.1
  • 13
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • N. Grigorieff FREALIGN: high-resolution refinement of single particle structures J. Struct. Biol. 157 2007 117 125
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 14
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • N. Grigorieff, and S.C. Harrison Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy Curr. Opin. Struct. Biol. 21 2011 265 273
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.2
  • 15
    • 0018333925 scopus 로고
    • Radiation damage of purple membrane at low temperature
    • S.B. Hayward, and R.M. Glaeser Radiation damage of purple membrane at low temperature Ultramicroscopy 04 1979 201 210
    • (1979) Ultramicroscopy , vol.4 , pp. 201-210
    • Hayward, S.B.1    Glaeser, R.M.2
  • 16
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • R. Henderson The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules Q. Rev. Biophys. 28 1995 171 193
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 17
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • R. Henderson, J.M. Baldwin, T.A. Ceska, F. Zemlin, E. Beckmann, and K.H. Downing Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213 1990 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
  • 19
    • 0035783389 scopus 로고    scopus 로고
    • Alignment error envelopes for single particle analysis
    • G.J. Jensen Alignment error envelopes for single particle analysis J. Struct. Biol. 133 2001 143 155
    • (2001) J. Struct. Biol. , vol.133 , pp. 143-155
    • Jensen, G.J.1
  • 20
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • W. Kühlbrandt, D.N. Wang, and Y. Fujiyoshi Atomic model of plant light-harvesting complex by electron crystallography Nature 367 1994 614 621
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 22
    • 77349116567 scopus 로고    scopus 로고
    • X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A resolution
    • B. McClain, E. Settembre, B.R. Temple, A.R. Bellamy, and S.C. Harrison X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A resolution J. Mol. Biol. 397 2010 587 599
    • (2010) J. Mol. Biol. , vol.397 , pp. 587-599
    • McClain, B.1    Settembre, E.2    Temple, B.R.3    Bellamy, A.R.4    Harrison, S.C.5
  • 23
    • 67650544797 scopus 로고    scopus 로고
    • Detective quantum efficiency of electron area detectors in electron microscopy
    • G. McMullan, S. Chen, R. Henderson, and A.R. Faruqi Detective quantum efficiency of electron area detectors in electron microscopy Ultramicroscopy 109 2009 1126 1143
    • (2009) Ultramicroscopy , vol.109 , pp. 1126-1143
    • McMullan, G.1    Chen, S.2    Henderson, R.3    Faruqi, A.R.4
  • 25
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • J.A. Mindell, and N. Grigorieff Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 26
    • 77955337464 scopus 로고    scopus 로고
    • Design of an electron microscope phase plate using a focused continuous-wave laser
    • 10.1088/1367-2630/12/7/073011
    • H. Muller, J. Jin, R. Danev, J. Spence, H. Padmore, and R.M. Glaeser Design of an electron microscope phase plate using a focused continuous-wave laser New J. Physics 12 2010 073011 10.1088/1367-2630/12/7/073011
    • (2010) New J. Physics , vol.12 , pp. 073011
    • Muller, H.1    Jin, J.2    Danev, R.3    Spence, J.4    Padmore, H.5    Glaeser, R.M.6
  • 27
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • E. Nogales, S.G. Wolf, and K.H. Downing Structure of the alpha beta tubulin dimer by electron crystallography Nature 391 1998 199 203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 28
    • 80855133523 scopus 로고    scopus 로고
    • Identifying conformational states of macromolecules by eigen-analysis of resampled cryo-EM images
    • P.A. Penczek, M. Kimmel, and C.M. Spahn Identifying conformational states of macromolecules by eigen-analysis of resampled cryo-EM images Structure 19 2011 1582 1590
    • (2011) Structure , vol.19 , pp. 1582-1590
    • Penczek, P.A.1    Kimmel, M.2    Spahn, C.M.3
  • 30
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 31
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: A fresh look at tobacco mosaic virus
    • C. Sachse, J.Z. Chen, P.D. Coureux, M.E. Stroupe, M. Fändrich, and N. Grigorieff High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus J. Mol. Biol. 371 2007 812 835
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.Z.2    Coureux, P.D.3    Stroupe, M.E.4    Fändrich, M.5    Grigorieff, N.6
  • 33
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • A. Stewart, and N. Grigorieff Noise bias in the refinement of structures derived from single particles Ultramicroscopy 102 2004 67 84
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 34
    • 0019991062 scopus 로고
    • Sequence diversity of human rotavirus strains investigated by northern blot hybridization analysis
    • J.E. Street, M.C. Croxson, W.F. Chadderton, and A.R. Bellamy Sequence diversity of human rotavirus strains investigated by northern blot hybridization analysis J. Virol. 43 1982 369 378
    • (1982) J. Virol. , vol.43 , pp. 369-378
    • Street, J.E.1    Croxson, M.C.2    Chadderton, W.F.3    Bellamy, A.R.4
  • 37
    • 84944439230 scopus 로고
    • Zur Defokussierungsabhängigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung [Defocus dependence of the phase contrast in the electron microscopic image]
    • F. Thon Zur Defokussierungsabhängigkeit des Phasenkontrastes bei der elektronenmikroskopischen Abbildung [Defocus dependence of the phase contrast in the electron microscopic image] Zeitschrift für Naturforschung 21a 1966 476 478
    • (1966) Zeitschrift für Naturforschung , vol.21 A , pp. 476-478
    • Thon, F.1
  • 38
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4A resolution J. Mol. Biol. 346 2005 967 989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 39
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • K. Yonekura, S. Maki-Yonekura, and K. Namba Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy Nature 424 2003 643 650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.