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Volumn 413, Issue 5, 2011, Pages 1028-1046

Tilt-pair analysis of images from a range of different specimens in single-particle electron cryomicroscopy

Author keywords

beam induced specimen motion; electron microscopy; particle orientation; radiation damage; structure validation

Indexed keywords

ACCURACY; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; IMAGE ANALYSIS; IMAGE QUALITY; MOLECULAR WEIGHT; PRIORITY JOURNAL; SINGLE PARTICLE ELECTRON CRYOMICROSCOPY; TEMPERATURE DEPENDENCE; TILT PAIR ANALYSIS; UNCERTAINTY;

EID: 80855132610     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.008     Document Type: Article
Times cited : (121)

References (66)
  • 1
    • 0000668797 scopus 로고
    • Reconstruction of three dimensional structures from electron micrographs
    • DeRosier D.J., and Klug A. Reconstruction of three dimensional structures from electron micrographs Nature 217 1968 130 134
    • (1968) Nature , vol.217 , pp. 130-134
    • Derosier, D.J.1    Klug, A.2
  • 2
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A., Amos L.A., Finch J.T., De Rosier D.J., and Klug A. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs Nature 226 1970 421 425
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    De Rosier, D.J.4    Klug, A.5
  • 3
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., and Unwin P.N.T. Three-dimensional model of purple membrane obtained by electron microscopy Nature 257 1975 28 32
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 4
    • 0023319667 scopus 로고
    • Three-dimensional structure of the large ribosomal subunit from Escherichia coli
    • Radermacher M., Wagenknecht T., Verschoor A., and Frank J. Three-dimensional structure of the large ribosomal subunit from Escherichia coli EMBO J. 6 1987 1107 1114
    • (1987) EMBO J. , vol.6 , pp. 1107-1114
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 6
    • 0022684837 scopus 로고
    • Three-dimensional structure of clathrin cages in ice
    • Vigers G.P., Crowther R.A., and Pearse B.M. Three-dimensional structure of clathrin cages in ice EMBO J. 5 1986 529 534
    • (1986) EMBO J. , vol.5 , pp. 529-534
    • Vigers, G.P.1    Crowther, R.A.2    Pearse, B.M.3
  • 7
    • 3142655417 scopus 로고    scopus 로고
    • Realizing the potential of electron cryo-microscopy
    • DOI 10.1017/S0033583504003920
    • Henderson R. Realizing the potential of electron cryo-microscopy Q. Rev. Biophys. 37 2004 3 13 (Pubitemid 38902192)
    • (2004) Quarterly Reviews of Biophysics , vol.37 , Issue.1 , pp. 3-13
    • Henderson, R.1
  • 8
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff N., and Harrison S.C. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy Curr. Opin. Struct. Biol. 21 2011 1 9
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 1-9
    • Grigorieff, N.1    Harrison, S.C.2
  • 9
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Å 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. 3.3 Å cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry Cell 141 2010 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
  • 10
    • 0017477892 scopus 로고
    • Motif detection in quantum noise limited electron micrographs by cross correlation
    • Saxton W.O., and Frank J. Motif detection in quantum noise-limited electron micrographs by cross-correlation Ultramicroscopy 2 1977 219 227 (Pubitemid 8130222)
    • (1977) Ultramicroscopy , vol.2 , Issue.2-3 , pp. 219-227
    • Saxton, W.O.1    Frank, J.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. 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
  • 12
    • 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. Images of paraffin monolayer crystals with perfect contrast: minimization of beam-induced specimen motion Ultramicroscopy 111 2011 90 100
    • (2011) Ultramicroscopy , vol.111 , pp. 90-100
    • Glaeser, R.M.1    McMullan, G.2    Faruqi, A.R.3    Henderson, R.4
  • 13
    • 79959668319 scopus 로고    scopus 로고
    • Reaching the information limit in cryo-EM of biological macromolecules: Experimental aspects
    • Glaeser R.M., and Hall R.J. Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects Biophys. J. 100 2011 2331 2337
    • (2011) Biophys. J. , vol.100 , pp. 2331-2337
    • Glaeser, R.M.1    Hall, R.J.2
  • 14
    • 77954650144 scopus 로고    scopus 로고
    • Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    • Fischer N., Konevega A.L., Wintermeyer W., Rodnina M.V., and Stark H. Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy Nature 466 2010 329 333
    • (2010) Nature , vol.466 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Wintermeyer, W.3    Rodnina, M.V.4    Stark, H.5
  • 15
    • 78650546283 scopus 로고    scopus 로고
    • Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution
    • Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., and Bhushan S. Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution Proc. Natl Acad. Sci. USA 107 2010 19748 19753
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 19748-19753
    • Armache, J.P.1    Jarasch, A.2    Anger, A.M.3    Villa, E.4    Becker, T.5    Bhushan, S.6
  • 16
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • DOI 10.1016/j.ultramic.2004.08.008, PII S0304399104001706
    • Stewart A., and Grigorieff N. Noise bias in the refinement of structures derived from single particles Ultramicroscopy 102 2004 67 84 (Pubitemid 39531897)
    • (2004) Ultramicroscopy , vol.102 , Issue.1 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 17
    • 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. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli J. Microsc. 146 1987 113 136
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 18
    • 32544460568 scopus 로고    scopus 로고
    • The orthogonal tilt reconstruction method: An approach to generating single-class volumes with no missing cone for ab initio reconstruction of asymmetric particles
    • DOI 10.1016/j.jsb.2005.10.012, PII S1047847705002339
    • Leschziner A.E., and Nogales E. The orthogonal tilt reconstruction method: an approach to generating single-class volumes with no missing cone for ab initio reconstruction of asymmetric particles J. Struct. Biol. 153 2006 284 299 (Pubitemid 43238321)
    • (2006) Journal of Structural Biology , vol.153 , Issue.3 , pp. 284-299
    • Leschziner, A.E.1    Nogales, E.2
  • 19
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • DOI 10.1083/jcb.127.2.411
    • Radermacher M., Rao V., Grassucci R., Frank J., Timerman A.P., Fleischer S., and Wagenknecht T. Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel-ryanodine receptor from skeletal muscle J. Cell Biol. 127 1994 411 423 (Pubitemid 24313730)
    • (1994) Journal of Cell Biology , vol.127 , Issue.2 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3    Frank, J.4    Timerman, A.P.5    Fleischer, S.6    Wagenknecht, T.7
  • 20
    • 0035782688 scopus 로고    scopus 로고
    • The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles
    • Ruiz T., Kopperschlager G., and Radermacher M. The first three-dimensional structure of phosphofructokinase from Saccharomyces cerevisiae determined by electron microscopy of single particles J. Struct. Biol. 136 2001 167 180
    • (2001) J. Struct. Biol. , vol.136 , pp. 167-180
    • Ruiz, T.1    Kopperschlager, G.2    Radermacher, M.3
  • 21
    • 84944295787 scopus 로고
    • Three-dimensional electron microscopy of individual biological objects. Part III. Experimental results on yeast fatty acid synthetase
    • Hoppe W., Schramm H.J., Sturm M., Hunsmann N., and Gassmann J. Three-dimensional electron microscopy of individual biological objects. Part III. Experimental results on yeast fatty acid synthetase Z. Naturforsch. 31a 1976 1380 1390
    • (1976) Z. Naturforsch. , vol.31 A , pp. 1380-1390
    • Hoppe, W.1    Schramm, H.J.2    Sturm, M.3    Hunsmann, N.4    Gassmann, J.5
  • 22
    • 0020536972 scopus 로고
    • Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs
    • Oettl H., Hegerl R., and Hoppe W. Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs J. Mol. Biol. 163 1983 431 450 (Pubitemid 13116446)
    • (1983) Journal of Molecular Biology , vol.163 , Issue.3 , pp. 431-450
    • Oettl, H.1    Hegerl, R.2    Hoppe, W.3
  • 25
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • DOI 10.1126/science.277.5332.1676
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., and Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases Science 277 1997 1676 1681 (Pubitemid 27446232)
    • (1997) Science , vol.277 , Issue.5332 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 26
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 A resolution
    • DOI 10.1016/S0969-2126(99)80118-X
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., and Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution Structure 7 1999 909 917 (Pubitemid 29372513)
    • (1999) Structure , vol.7 , Issue.8 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 27
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • Rosenthal P.B., and Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745 (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 28
    • 0345599153 scopus 로고    scopus 로고
    • Comparison of the Structures of Three Circoviruses: Chicken Anemia Virus, Porcine Circovirus Type 2, and Beak and Feather Disease Virus
    • DOI 10.1128/JVI.77.24.13036-13041.2003
    • Crowther R.A., Berriman J.A., Curran W.L., Allan G.M., and Todd D. Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus J. Virol. 77 2003 13036 13041 (Pubitemid 37494299)
    • (2003) Journal of Virology , vol.77 , Issue.24 , pp. 13036-13041
    • Crowther, R.A.1    Berriman, J.A.2    Curran, W.L.3    Allan, G.M.4    Todd, D.5
  • 29
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • DOI 10.1093/emboj/cdg608
    • Rubinstein J.L., Walker J.E., and Henderson R. Structure of the mitochondrial ATP synthase by electron cryomicroscopy EMBO J. 22 2003 6182 6192 (Pubitemid 37522576)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 30
    • 40049096125 scopus 로고    scopus 로고
    • Cryo-EM Structure of the DNA-Dependent Protein Kinase Catalytic Subunit at Subnanometer Resolution Reveals α Helices and Insight into DNA Binding
    • DOI 10.1016/j.str.2007.12.014, PII S0969212608000208
    • Williams D.R., Lee K.J., Shi J., Chen D.J., and Stewart P.L. Cryo-EM structure of the DNA-dependent protein kinase catalytic subunit at subnanometer resolution reveals α helices and insight into DNA binding Structure 16 2008 468 477 (Pubitemid 351324109)
    • (2008) Structure , vol.16 , Issue.3 , pp. 468-477
    • Williams, D.R.1    Lee, K.-J.2    Shi, J.3    Chen, D.J.4    Stewart, P.L.5
  • 31
    • 76549094484 scopus 로고    scopus 로고
    • Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor
    • Lau W.C., and Rubinstein J.L. Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor Proc. Natl Acad. Sci. USA 107 2010 1367 1372
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1367-1372
    • Lau, W.C.1    Rubinstein, J.L.2
  • 32
    • 0037099293 scopus 로고    scopus 로고
    • +-ATPase: 3D structures of two states by electron cryo-microscopy
    • DOI 10.1093/emboj/cdf385
    • Rhee K.H., Scarborough G.A., and Henderson R. Domain movements of plasma membrane H(+)-ATPase: 3D structures of two states by electron cryo-microscopy EMBO J. 21 2002 3582 3589 (Pubitemid 34787032)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3582-3589
    • Rhee, K.-H.1    Scarborough, G.A.2    Henderson, R.3
  • 34
    • 37449008520 scopus 로고    scopus 로고
    • Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    • Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S., and Saibil H.R. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104 Cell 131 2007 1366 1377
    • (2007) Cell , vol.131 , pp. 1366-1377
    • Wendler, P.1    Shorter, J.2    Plisson, C.3    Cashikar, A.G.4    Lindquist, S.5    Saibil, H.R.6
  • 35
    • 51349153212 scopus 로고    scopus 로고
    • Cryo-EM structure of the yeast ATP synthase
    • Lau W.C., Baker L.A., and Rubinstein J.L. Cryo-EM structure of the yeast ATP synthase J. Mol. Biol. 382 2008 1256 1264
    • (2008) J. Mol. Biol. , vol.382 , pp. 1256-1264
    • Lau, W.C.1    Baker, L.A.2    Rubinstein, J.L.3
  • 37
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (Complex I) at 22 A in ice
    • DOI 10.1006/jmbi.1998.1668
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 Å in ice J. Mol. Biol. 277 1998 1033 1046 (Pubitemid 28190844)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1033-1046
    • Grigorieff, N.1
  • 38
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: High-resolution refinement of single particle structures
    • DOI 10.1016/j.jsb.2006.05.004, PII S1047847706001699, Software Tools for Macromolecular Microscopy
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures J. Struct. Biol. 157 2007 117 125 (Pubitemid 44880784)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 117-125
    • Grigorieff, N.1
  • 39
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang G., Peng L., Baldwin P.R., Mann D.S., Jiang W., Rees I., and Ludtke S.J. EMAN2: an extensible image processing suite for electron microscopy J. Struct. Biol. 157 2007 38 46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 42
    • 0028178377 scopus 로고
    • Three-dimensional structure of β-galactosidase from E. coli
    • Jacobson R.H., Zhang X.J., DuBose R.F., and Matthews B.W. Three-dimensional structure of β-galactosidase from E. coli Nature 369 1994 761 766
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    Dubose, R.F.3    Matthews, B.W.4
  • 43
    • 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. 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 2010 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
  • 45
    • 77952719956 scopus 로고    scopus 로고
    • Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy
    • Gipson P., Mills D.J., Wouts R., Grininger M., Vonck J., and Kuhlbrandt W. Direct structural insight into the substrate-shuttling mechanism of yeast fatty acid synthase by electron cryomicroscopy Proc. Natl Acad. Sci. USA 107 2010 9164 9169
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9164-9169
    • Gipson, P.1    Mills, D.J.2    Wouts, R.3    Grininger, M.4    Vonck, J.5    Kuhlbrandt, W.6
  • 46
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • DOI 10.1016/S1047-8477(03)00069-8
    • Mindell J.A., and Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347 (Pubitemid 36638267)
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 47
    • 79960133051 scopus 로고    scopus 로고
    • Electronic detectors for electron microscopy
    • Faruqi A.R., and McMullan G. Electronic detectors for electron microscopy Q. Rev. Biophys. 44 2011 357 390
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 357-390
    • Faruqi, A.R.1    McMullan, G.2
  • 48
    • 38349081491 scopus 로고    scopus 로고
    • Single particle analysis based on Zernike phase contrast transmission electron microscopy
    • Danev R., and Nagayama K. Single particle analysis based on Zernike phase contrast transmission electron microscopy J. Struct. Biol. 161 2008 211 218
    • (2008) J. Struct. Biol. , vol.161 , pp. 211-218
    • Danev, R.1    Nagayama, K.2
  • 49
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy
    • Crowther R.A., DeRosier D.J., and Klug A. The reconstruction of a three-dimensional structure from projections and its application to electron microscopy Proc. R. Soc. London, Ser. A 317 1970 319 340
    • (1970) Proc. R. Soc. London, Ser. A , vol.317 , pp. 319-340
    • Crowther, R.A.1    Derosier, D.J.2    Klug, A.3
  • 50
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • DOI 10.1038/35018597
    • Frank J., and Agrawal R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation Nature 406 2000 318 322 (Pubitemid 30604411)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 51
    • 4344605740 scopus 로고    scopus 로고
    • Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset
    • DOI 10.1016/j.jsb.2004.02.008, PII S1047847704000437
    • Gao H., Valle M., Ehrenberg M., and Frank J. Dynamics of EF-G interaction with the ribosome explored by classification of a heterogeneous cryo-EM dataset J. Struct. Biol. 147 2004 283 290 (Pubitemid 39140735)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 283-290
    • Gao, H.1    Valle, M.2    Ehrenberg, M.3    Frank, J.4
  • 53
    • 32544442151 scopus 로고    scopus 로고
    • Observations on the behavior of vitreous ice at ∼82 and∼12 K
    • DOI 10.1016/j.jsb.2005.12.003, PII S1047847705002893
    • Wright E.R., Iancu C.V., Tivol W.F., and Jensen G.J. Observations on the behavior of vitreous ice at approximately 82 and approximately 12 K J. Struct. Biol. 153 2006 241 252 (Pubitemid 43238317)
    • (2006) Journal of Structural Biology , vol.153 , Issue.3 , pp. 241-252
    • Wright, E.R.1    Iancu, C.V.2    Tivol, W.F.3    Jensen, G.J.4
  • 54
    • 75749092651 scopus 로고    scopus 로고
    • Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures
    • Meents A., Gutmann S., Wagner A., and Schulze-Briese C. Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures Proc. Natl Acad. Sci. USA 107 2010 1094 1099
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1094-1099
    • Meents, A.1    Gutmann, S.2    Wagner, A.3    Schulze-Briese, C.4
  • 57
    • 0030174932 scopus 로고    scopus 로고
    • Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures
    • DOI 10.1016/0304-3991(96)00045-9
    • Stark H., Zemlin F., and Boettcher C. Electron radiation damage to protein crystals of bacteriorhodopsin at different temperatures Ultramicroscopy 63 1996 75 79 (Pubitemid 26336686)
    • (1996) Ultramicroscopy , vol.63 , Issue.2 , pp. 75-79
    • Stark, H.1    Zemlin, F.2    Boettcher, C.3
  • 58
    • 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. 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
  • 59
    • 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. 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
  • 62
    • 33845600388 scopus 로고    scopus 로고
    • Digitisation of electron microscope films: Six useful tests applied to three film scanners
    • DOI 10.1016/j.ultramic.2006.05.003, PII S030439910600088X
    • Henderson R., Cattermole D., McMullan G., Scotcher S., Fordham M., Amos W.B., and Faruqi A.R. Digitisation of electron microscope films: six useful tests applied to three film scanners Ultramicroscopy 107 2007 73 80 (Pubitemid 44959441)
    • (2007) Ultramicroscopy , vol.107 , Issue.2-3 , pp. 73-80
    • Henderson, R.1    Cattermole, D.2    McMullan, G.3    Scotcher, S.4    Fordham, M.5    Amos, W.B.6    Faruqi, A.R.7
  • 63
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp - A visualization tool to aid structure determination from electron microscope images
    • DOI 10.1006/jsbi.1998.4073
    • Smith J.M. Ximdisp-a visualization tool to aid structure determination from electron microscope images J. Struct. Biol. 125 1999 223 228 (Pubitemid 29402607)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 223-228
    • Smith, J.M.1
  • 66
    • 84944439230 scopus 로고
    • On the defocusing dependence of phase contrast in electron microscopical images
    • Thon F. On the defocusing dependence of phase contrast in electron microscopical images Z. Naturforsch. 21 1966 476 478
    • (1966) Z. Naturforsch. , vol.21 , pp. 476-478
    • Thon, F.1


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