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Volumn 1, Issue , 2012, Pages 245-276

Structure determination of macromolecular complexes by cryo-electron microscopy in vitro and in situ

Author keywords

Chaperone; Cryo electron microscopy; Cryo electron tomography; Electron microscopy; Macromolecular complex; Modeling; Protease; Ribosome; Single particle analysis; Structural biology

Indexed keywords


EID: 84882784462     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00118-1     Document Type: Chapter
Times cited : (3)

References (254)
  • 1
    • 0842334536 scopus 로고    scopus 로고
    • Whither structural biology?
    • Harrison S.C. Whither structural biology?. Nat. Struct. Mol. Biol. 2004, 11(1):12-15.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , Issue.1 , pp. 12-15
    • Harrison, S.C.1
  • 3
    • 0037435031 scopus 로고    scopus 로고
    • From words to literature in structural proteomics
    • Sali A., Glaeser R., Earnest T., Baumeister W. From words to literature in structural proteomics. Nature 2003, 422(6928):216-225.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 216-225
    • Sali, A.1    Glaeser, R.2    Earnest, T.3    Baumeister, W.4
  • 4
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 1998, 92(3):291-294.
    • (1998) Cell , vol.92 , Issue.3 , pp. 291-294
    • Alberts, B.1
  • 5
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson C.V., Sali A., Baumeister W. The molecular sociology of the cell. Nature 2007, 450(7172):973-982.
    • (2007) Nature , vol.450 , Issue.7172 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 6
    • 70350292376 scopus 로고    scopus 로고
    • Post-reductionist protein science, or putting Humpty Dumpty back together again
    • Gierasch L.M., Gershenson A. Post-reductionist protein science, or putting Humpty Dumpty back together again. Nat. Chem. Biol. 2009, 5(11):774-777.
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.11 , pp. 774-777
    • Gierasch, L.M.1    Gershenson, A.2
  • 8
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic V., Forster F., Baumeister W. Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 2005, 74:833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 9
    • 77957941761 scopus 로고    scopus 로고
    • Focal issue on hybrid imaging
    • Plitzko J., Baumeister W. Focal issue on hybrid imaging. J. Struct. Biol. 2010, 172(2):159.
    • (2010) J. Struct. Biol. , vol.172 , Issue.2 , pp. 159
    • Plitzko, J.1    Baumeister, W.2
  • 12
    • 0040310859 scopus 로고
    • Molecular microscopy: fundamental limitations
    • Breedlove J.R., Trammell G.T. Molecular microscopy: fundamental limitations. Science 1970, 170:1310-1313.
    • (1970) Science , vol.170 , pp. 1310-1313
    • Breedlove, J.R.1    Trammell, G.T.2
  • 13
    • 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(2):171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , Issue.2 , pp. 171-193
    • Henderson, R.1
  • 14
    • 0030199056 scopus 로고    scopus 로고
    • Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging
    • Grimm R., Typke D., Barmann M., Baumeister W. Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging. Ultramicroscopy 1996, 63(3-4):169-179.
    • (1996) Ultramicroscopy , vol.63 , Issue.3-4 , pp. 169-179
    • Grimm, R.1    Typke, D.2    Barmann, M.3    Baumeister, W.4
  • 15
    • 0016391518 scopus 로고
    • Electron diffraction of frozen, hydrated protein crystals
    • Taylor K.A., Glaeser R.M. Electron diffraction of frozen, hydrated protein crystals. Science 1974, 186(4168):1036-1037.
    • (1974) Science , vol.186 , Issue.4168 , pp. 1036-1037
    • Taylor, K.A.1    Glaeser, R.M.2
  • 19
    • 77957225478 scopus 로고    scopus 로고
    • Phase plates for transmission electron microscopy
    • Danev R., Nagayama K. Phase plates for transmission electron microscopy. Methods Enzymol. 2010, 481:343-369.
    • (2010) Methods Enzymol. , vol.481 , pp. 343-369
    • Danev, R.1    Nagayama, K.2
  • 20
    • 0026566945 scopus 로고
    • A brief look at imaging and contrast transfer
    • Wade R.H. A brief look at imaging and contrast transfer. Ultramicroscopy 1992, 46(1-4):145-156.
    • (1992) Ultramicroscopy , vol.46 , Issue.1-4 , pp. 145-156
    • Wade, R.H.1
  • 21
    • 0027405822 scopus 로고
    • Contrast transfer for frozen-hydrated specimens. II. Amplitude contrast at very low frequencies
    • Toyoshima C., Yonekura K., Sasabe H. Contrast transfer for frozen-hydrated specimens. II. Amplitude contrast at very low frequencies. Ultramicroscopy 1993, 48:165-176.
    • (1993) Ultramicroscopy , vol.48 , pp. 165-176
    • Toyoshima, C.1    Yonekura, K.2    Sasabe, H.3
  • 22
    • 77957305562 scopus 로고    scopus 로고
    • Image restoration in cryo-electron microscopy
    • Penczek P.A. Image restoration in cryo-electron microscopy. Methods Enzymol. 2010, 482:35-72.
    • (2010) Methods Enzymol. , vol.482 , pp. 35-72
    • Penczek, P.A.1
  • 23
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128(1):82-97.
    • (1999) J. Struct. Biol. , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 24
    • 0030960710 scopus 로고    scopus 로고
    • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome
    • Zhu J., Penczek P.A., Schroder R., Frank J. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 1997, 118(3):197-219.
    • (1997) J. Struct. Biol. , vol.118 , Issue.3 , pp. 197-219
    • Zhu, J.1    Penczek, P.A.2    Schroder, R.3    Frank, J.4
  • 25
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 A in ice. J. Mol. Biol. 1998, 277(5):1033-1046.
    • (1998) J. Mol. Biol. , vol.277 , Issue.5 , pp. 1033-1046
    • Grigorieff, N.1
  • 26
    • 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. Journal of Structural Biology 2003, 142(3):334-347.
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 27
    • 33646784015 scopus 로고    scopus 로고
    • CTF determination and correction in electron cryotomography
    • Fernandez J.J., Li S., Crowther R.A. CTF determination and correction in electron cryotomography. Ultramicroscopy 2006, 106(7):587-596.
    • (2006) Ultramicroscopy , vol.106 , Issue.7 , pp. 587-596
    • Fernandez, J.J.1    Li, S.2    Crowther, R.A.3
  • 28
    • 70349467745 scopus 로고    scopus 로고
    • Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging
    • Zanetti G., Riches J.D., Fuller S.D., Briggs J.A. Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging. J. Struct. Biol. 2009, 168(2):305-312.
    • (2009) J. Struct. Biol. , vol.168 , Issue.2 , pp. 305-312
    • Zanetti, G.1    Riches, J.D.2    Fuller, S.D.3    Briggs, J.A.4
  • 29
    • 0001169360 scopus 로고
    • Über die Bestimmung von Funktionen durch ihre Integralwerte längs gewisser Mannigfaltigkeiten
    • Radon J. Über die Bestimmung von Funktionen durch ihre Integralwerte längs gewisser Mannigfaltigkeiten. Berichte Sächsische Akadamie der Wissenschaften, Leipzig, Math.-Phys. Kl 1917, 69:262-277.
    • (1917) Berichte Sächsische Akadamie der Wissenschaften, Leipzig, Math.-Phys. Kl , vol.69 , pp. 262-277
    • Radon, J.1
  • 30
    • 0002595460 scopus 로고
    • The electron microscope as a structure projector
    • Plenum Press, New York, J. Frank (Ed.)
    • Hawkes P.W. The electron microscope as a structure projector. Electron Tomography 1992, 17-38. Plenum Press, New York. J. Frank (Ed.).
    • (1992) Electron Tomography , pp. 17-38
    • Hawkes, P.W.1
  • 31
    • 0019363273 scopus 로고
    • Three-dimensional electron microscopy
    • Hoppe W. Three-dimensional electron microscopy. Annu. Rev. Biophys. Bioeng. 1981, 10:563-592.
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 563-592
    • Hoppe, W.1
  • 32
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from its projections and its applications to electron microscopy
    • Crowther R.A., DeRosier D.J., Klug A. The reconstruction of a three-dimensional structure from its projections and its applications to electron microscopy. Proceedings of the Royal Society, London 1970, 317:319-340.
    • (1970) Proceedings of the Royal Society, London , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 34
    • 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
  • 35
    • 77957315907 scopus 로고    scopus 로고
    • Fundamentals of three-dimensional reconstruction from projections
    • Penczek P.A. Fundamentals of three-dimensional reconstruction from projections. Methods Enzymol. 2010, 482:1-33.
    • (2010) Methods Enzymol. , vol.482 , pp. 1-33
    • Penczek, P.A.1
  • 36
    • 0011968859 scopus 로고
    • Three-dimensional structure determination by electron microscopy (nonperiodic specimens)
    • Springer-Verlag, Berlin Heidelberg New York
    • Hoppe W., Hegerl R. Three-dimensional structure determination by electron microscopy (nonperiodic specimens). Computer Processing of Electron Microscope Images 1980, Vol. 13:127-185. Springer-Verlag, Berlin Heidelberg New York.
    • (1980) Computer Processing of Electron Microscope Images , vol.13 , pp. 127-185
    • Hoppe, W.1    Hegerl, R.2
  • 37
    • 2042540051 scopus 로고    scopus 로고
    • Gridding-based direct Fourier inversion of the three-dimensional ray transform
    • Penczek P.A., Renka R., Schomberg H. Gridding-based direct Fourier inversion of the three-dimensional ray transform. J. Opt. Soc. Am. A. Opt. Image Sci. Vis. 2004, 21(4):499-509.
    • (2004) J. Opt. Soc. Am. A. Opt. Image Sci. Vis. , vol.21 , Issue.4 , pp. 499-509
    • Penczek, P.A.1    Renka, R.2    Schomberg, H.3
  • 38
    • 57049145347 scopus 로고    scopus 로고
    • Heterogeneity of large macromolecular complexes revealed by 3-D cryo-EM variance analysis
    • Zhang W., Kimmel M., Spahn C.M., Penczek P.A. Heterogeneity of large macromolecular complexes revealed by 3-D cryo-EM variance analysis. Structure 2008, 16(12):1770-1776.
    • (2008) Structure , vol.16 , Issue.12 , pp. 1770-1776
    • Zhang, W.1    Kimmel, M.2    Spahn, C.M.3    Penczek, P.A.4
  • 39
    • 77958185624 scopus 로고    scopus 로고
    • Ab initio high-resolution single-particle 3-D reconstructions: the symmetry adapted functions way
    • Estrozi L.F., Navaza J. Ab initio high-resolution single-particle 3-D reconstructions: the symmetry adapted functions way. J. Struct. Biol. 2010, 172:253-260.
    • (2010) J. Struct. Biol. , vol.172 , pp. 253-260
    • Estrozi, L.F.1    Navaza, J.2
  • 41
    • 0014905513 scopus 로고
    • Algebraic reconstruction techniques (ART) for three-dimensional electron microscopy
    • Gordon R., Bender R., Herman G.T. Algebraic reconstruction techniques (ART) for three-dimensional electron microscopy. J. Theor. Biol. 1970, 29:471-481.
    • (1970) J. Theor. Biol. , vol.29 , pp. 471-481
    • Gordon, R.1    Bender, R.2    Herman, G.T.3
  • 42
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 1992, 40:33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 44
    • 0032053763 scopus 로고    scopus 로고
    • 3-D reconstruction in electron microscopy using ART with smooth spherically symmetric volume elements (blobs)
    • Marabini R., Herman G.T., Carazo J.M. 3-D reconstruction in electron microscopy using ART with smooth spherically symmetric volume elements (blobs). Ultramicroscopy 1998, 72(1-2):53-65.
    • (1998) Ultramicroscopy , vol.72 , Issue.1-2 , pp. 53-65
    • Marabini, R.1    Herman, G.T.2    Carazo, J.M.3
  • 46
    • 0027540566 scopus 로고
    • Applications of slow-scan CCD cameras in transmission electron microscopy
    • Krivanek O.L., Mooney P.E. Applications of slow-scan CCD cameras in transmission electron microscopy. Ultramicroscopy 1993, 49:95-108.
    • (1993) Ultramicroscopy , vol.49 , pp. 95-108
    • Krivanek, O.L.1    Mooney, P.E.2
  • 47
    • 10744220292 scopus 로고    scopus 로고
    • Automated image acquisition and processing using a new generation of 4K×4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies
    • Zhang P., Borgnia M.J., Mooney P., Shi D., Pan M., O'Herron P., Mao A., Brogan D., Milne J.L., Subramaniam S. Automated image acquisition and processing using a new generation of 4K×4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies. J. Struct. Biol. 2003, 143(2):135-144.
    • (2003) J. Struct. Biol. , vol.143 , Issue.2 , pp. 135-144
    • Zhang, P.1    Borgnia, M.J.2    Mooney, P.3    Shi, D.4    Pan, M.5    O'Herron, P.6    Mao, A.7    Brogan, D.8    Milne, J.L.9    Subramaniam, S.10
  • 48
    • 67650544797 scopus 로고    scopus 로고
    • Detective quantum efficiency of electron area detectors in electron microscopy
    • McMullan G., Chen S., Henderson R., Faruqi A.R. Detective quantum efficiency of electron area detectors in electron microscopy. Ultramicroscopy 2009, 109(9):1126-1143.
    • (2009) Ultramicroscopy , vol.109 , Issue.9 , pp. 1126-1143
    • McMullan, G.1    Chen, S.2    Henderson, R.3    Faruqi, A.R.4
  • 51
    • 0026566946 scopus 로고
    • Automated microscopy for electron tomography
    • Koster A.J., Chen H., Sedat J.W., Agard D.A. Automated microscopy for electron tomography. Ultramicroscopy 1992, 46(1-4):207-227.
    • (1992) Ultramicroscopy , vol.46 , Issue.1-4 , pp. 207-227
    • Koster, A.J.1    Chen, H.2    Sedat, J.W.3    Agard, D.A.4
  • 52
    • 0032127262 scopus 로고    scopus 로고
    • Automation of specimen selection and data acquisition for protein electron crystallography
    • Oostergetel G.T., Keegstra W., Brisson A. Automation of specimen selection and data acquisition for protein electron crystallography. Ultramicroscopy 1998, 74(1-2):47-59.
    • (1998) Ultramicroscopy , vol.74 , Issue.1-2 , pp. 47-59
    • Oostergetel, G.T.1    Keegstra, W.2    Brisson, A.3
  • 56
  • 58
    • 51549098155 scopus 로고    scopus 로고
    • Microscopy (SAM) package to improve data acquisition rates on FEI Tecnai electron microscopes equipped with Gatan CCD cameras
    • Shi J., Williams D.R., Stewart P.L., Script-Assisted A Microscopy (SAM) package to improve data acquisition rates on FEI Tecnai electron microscopes equipped with Gatan CCD cameras. J. Struct. Biol. 2008, 164(1):166-169.
    • (2008) J. Struct. Biol. , vol.164 , Issue.1 , pp. 166-169
    • Shi, J.1    Williams, D.R.2    Stewart, P.L.3    Script-Assisted, A.4
  • 60
    • 77449108419 scopus 로고    scopus 로고
    • Single-particle reconstruction of biological macromolecules in electron microscopy - 30 years
    • Frank J. Single-particle reconstruction of biological macromolecules in electron microscopy - 30 years. Q. Rev. Biophys. 2009, 42(3):139-158.
    • (2009) Q. Rev. Biophys. , vol.42 , Issue.3 , pp. 139-158
    • Frank, J.1
  • 61
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • Leake M.C., Chandler J.H., Wadhams G.H., Bai F., Berry R.M., Armitage J.P. Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 2006, 443(7109):355-358.
    • (2006) Nature , vol.443 , Issue.7109 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 62
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DeRosier D.J., Klug A. Reconstruction of three-dimensional structures from electron micrographs. Nature 1968, 217:130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 64
    • 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(3):441-448.
    • (2008) Structure , vol.16 , Issue.3 , 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
  • 65
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • Yu X., Jin L., Zhou Z.H. 3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 2008, 453(7193):415-419.
    • (2008) Nature , vol.453 , Issue.7193 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 68
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Bottcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386(6620):88-91.
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 69
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • Conway J.F., Cheng N., Zlotnick A., Wingfield P.T., Stahl S.J., Steven A.C. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature 1997, 386(6620):91-94.
    • (1997) Nature , vol.386 , Issue.6620 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingfield, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 70
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial-cell envelope protein
    • Saxton W.O., Baumeister W. The correlation averaging of a regularly arranged bacterial-cell envelope protein. J. Microsc.-Oxford 1982, 127(Aug):127-138.
    • (1982) J. Microsc.-Oxford , vol.127 , Issue.AUG , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 71
    • 77957296661 scopus 로고    scopus 로고
    • Resolution measures in molecular electron microscopy
    • Penczek P.A. Resolution measures in molecular electron microscopy. Methods Enzymol. 2010, 482:73-100.
    • (2010) Methods Enzymol. , vol.482 , pp. 73-100
    • Penczek, P.A.1
  • 72
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 2003, 333(4):721-745.
    • (2003) J. Mol. Biol. , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 73
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff N. Resolution measurement in structures derived from single particles. Acta Crystallogr. D Biol. Crystallogr. 2000, 56(Pt 10):1270-1277.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PT 10 , pp. 1270-1277
    • Grigorieff, N.1
  • 74
    • 11144246307 scopus 로고    scopus 로고
    • Unified 3-D structure and projection orientation refinement using quasi-Newton algorithm
    • Yang C., Ng E.G., Penczek P.A. Unified 3-D structure and projection orientation refinement using quasi-Newton algorithm. J. Struct. Biol. 2005, 149(1):53-64.
    • (2005) J. Struct. Biol. , vol.149 , Issue.1 , pp. 53-64
    • Yang, C.1    Ng, E.G.2    Penczek, P.A.3
  • 75
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3-D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. SPIDER and WEB: processing and visualization of images in 3-D electron microscopy and related fields. J. Struct. Biol. 1996, 116(1):190-199.
    • (1996) J. Struct. Biol. , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 76
  • 79
    • 0019728717 scopus 로고
    • Use of multivariate statistics in analysing the images of biological macromolecules
    • van Heel M., Frank J. Use of multivariate statistics in analysing the images of biological macromolecules. Ultramicroscopy 1981, 6:187-194.
    • (1981) Ultramicroscopy , vol.6 , pp. 187-194
    • van Heel, M.1    Frank, J.2
  • 80
    • 0023102907 scopus 로고
    • Angular reconstitution: a posteriori assignment of projection directions for 3-D reconstruction
    • Van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3-D reconstruction. Ultramicroscopy 1987, 21(2):111-123.
    • (1987) Ultramicroscopy , vol.21 , Issue.2 , pp. 111-123
    • Van Heel, M.1
  • 81
    • 0023102907 scopus 로고
    • Angular reconstitution: a posteriori assignment of projection directions for 3-D reconstructions
    • van Heel M. Angular reconstitution: a posteriori assignment of projection directions for 3-D reconstructions. Ultramicroscopy 1987, 21:111-124.
    • (1987) Ultramicroscopy , vol.21 , pp. 111-124
    • van Heel, M.1
  • 82
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from single-exposure random conical tilt series applied to the 50S ribosomal subunit of Eschericia coli
    • Radermacher M., Wagenknecht T., Verschoor A., Frank J. Three-dimensional reconstruction from single-exposure random conical tilt series applied to the 50S ribosomal subunit of Eschericia coli. Journal of Microscopy 1987, 146:113-136.
    • (1987) Journal of Microscopy , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 83
    • 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
    • Leschziner A.E., 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. 2006, 153(3):284-299.
    • (2006) J. Struct. Biol. , vol.153 , Issue.3 , pp. 284-299
    • Leschziner, A.E.1    Nogales, E.2
  • 84
    • 0031423486 scopus 로고    scopus 로고
    • Electron tomography of single ice-embedded macromolecules: three-dimensional alignment and classification
    • Walz J., Typke D., Nitsch M., Koster A.J., Hegerl R., Baumeister W. Electron tomography of single ice-embedded macromolecules: three-dimensional alignment and classification. J. Struct. Biol. 1997, 120(3):387-395.
    • (1997) J. Struct. Biol. , vol.120 , Issue.3 , pp. 387-395
    • Walz, J.1    Typke, D.2    Nitsch, M.3    Koster, A.J.4    Hegerl, R.5    Baumeister, W.6
  • 85
    • 16344390563 scopus 로고    scopus 로고
    • Retrovirus envelope protein complex structure in situ determined by cryo-electron tomography
    • Förster F., Medalia O., Zauberman N., Baumeister W., Fass D. Retrovirus envelope protein complex structure in situ determined by cryo-electron tomography. Proc. Natl. Acad. Sci. USA 2005, 102(13):4729-4734.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.13 , pp. 4729-4734
    • Förster, F.1    Medalia, O.2    Zauberman, N.3    Baumeister, W.4    Fass, D.5
  • 86
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng Y., Zak O., Aisen P., Harrison S.C., Walz T. Structure of the human transferrin receptor-transferrin complex. Cell 2004, 116(4):565-576.
    • (2004) Cell , vol.116 , Issue.4 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 88
    • 0031704540 scopus 로고    scopus 로고
    • A maximum-likelihood approach to single-particle image refinement
    • Sigworth F.J. A maximum-likelihood approach to single-particle image refinement. J. Struct. Biol. 1998, 122(3):328-339.
    • (1998) J. Struct. Biol. , vol.122 , Issue.3 , pp. 328-339
    • Sigworth, F.J.1
  • 89
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3-D-EM through likelihood optimization
    • Epub 2006 Dec 10
    • Scheres S.H., Gao H., Valle M., Herman G.T., Eggermont P.P., Frank J., Carazo J.M. Disentangling conformational states of macromolecules in 3-D-EM through likelihood optimization. Nat. Methods 2007, 4(1):27-29. Epub 2006 Dec 10.
    • (2007) Nat. Methods , vol.4 , Issue.1 , pp. 27-29
    • Scheres, S.H.1    Gao, H.2    Valle, M.3    Herman, G.T.4    Eggermont, P.P.5    Frank, J.6    Carazo, J.M.7
  • 90
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann J.B., Cheng N., Newcomb W.W., Trus B.L., Brown J.C., Steven A.C. Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat. Struct. Biol. 2003, 10(5):334-341.
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.5 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 91
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • Marlovits T.C., Kubori T., SGBRhan A., Thomas D.R., Galan J.E., Unger V.M. Structural insights into the assembly of the type III secretion needle complex. Science 2004, 306(5698):1040-1042.
    • (2004) Science , vol.306 , Issue.5698 , pp. 1040-1042
    • Marlovits, T.C.1    Kubori, T.2    SGBRhan, A.3    Thomas, D.R.4    Galan, J.E.5    Unger, V.M.6
  • 93
    • 33749608423 scopus 로고    scopus 로고
    • The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium
    • Thomas D.R., Francis N.R., Xu C., DeRosier D.J. The three-dimensional structure of the flagellar rotor from a clockwise-locked mutant of Salmonella enterica serovar Typhimurium. J. Bacteriol. 2006, 188(20):7039-7048.
    • (2006) J. Bacteriol. , vol.188 , Issue.20 , pp. 7039-7048
    • Thomas, D.R.1    Francis, N.R.2    Xu, C.3    DeRosier, D.J.4
  • 94
    • 33646042904 scopus 로고    scopus 로고
    • A method of focused classification, based on the bootstrap 3-D variance analysis, and its application to EF-G-dependent translocation
    • Penczek P.A., Frank J., Spahn C.M. A method of focused classification, based on the bootstrap 3-D variance analysis, and its application to EF-G-dependent translocation. J. Struct. Biol. 2006, 154(2):184-194.
    • (2006) J. Struct. Biol. , vol.154 , Issue.2 , pp. 184-194
    • Penczek, P.A.1    Frank, J.2    Spahn, C.M.3
  • 95
    • 77953565575 scopus 로고    scopus 로고
    • An approach for de novo structure determination of dynamic molecular assemblies by electron cryomicroscopy
    • Sander B., Golas M.M., Luhrmann R., Stark H. An approach for de novo structure determination of dynamic molecular assemblies by electron cryomicroscopy. Structure 2010, 18(6):667-676.
    • (2010) Structure , vol.18 , Issue.6 , pp. 667-676
    • Sander, B.1    Golas, M.M.2    Luhrmann, R.3    Stark, H.4
  • 96
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., Agrawal R.K. A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 2000, 406(6793):318-322.
    • (2000) Nature , vol.406 , Issue.6793 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 97
    • 54049116765 scopus 로고    scopus 로고
    • Visualization of the hybrid state of tRNA binding promoted by spontaneous ratcheting of the ribosome
    • Agirrezabala X., Lei J., Brunelle J.L., Ortiz-Meoz R.F., Green R., Frank J. Visualization of the hybrid state of tRNA binding promoted by spontaneous ratcheting of the ribosome. Molecular Cell 2008, 32(2):190-197.
    • (2008) Molecular Cell , vol.32 , Issue.2 , pp. 190-197
    • Agirrezabala, X.1    Lei, J.2    Brunelle, J.L.3    Ortiz-Meoz, R.F.4    Green, R.5    Frank, J.6
  • 104
    • 49349091956 scopus 로고    scopus 로고
    • Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy
    • Sengupta J., Nilsson J., Gursky R., Kjeldgaard M., Nissen P., Frank J. Visualization of the eEF2-80S ribosome transition-state complex by cryo-electron microscopy. J. Mol. Biol. 2008, 382(1):179-187.
    • (2008) J. Mol. Biol. , vol.382 , Issue.1 , pp. 179-187
    • Sengupta, J.1    Nilsson, J.2    Gursky, R.3    Kjeldgaard, M.4    Nissen, P.5    Frank, J.6
  • 105
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic M., Becker T., Pool M.R., Spahn C.M., Grassucci R.A., Frank J., Beckmann R. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 2004, 427(6977):808-814.
    • (2004) Nature , vol.427 , Issue.6977 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 106
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I., Beckmann R. Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 2006, 444(7118):507-511.
    • (2006) Nature , vol.444 , Issue.7118 , pp. 507-511
    • Halic, M.1    Blau, M.2    Becker, T.3    Mielke, T.4    Pool, M.R.5    Wild, K.6    Sinning, I.7    Beckmann, R.8
  • 107
    • 33646442605 scopus 로고    scopus 로고
    • Signal recognition particle receptor exposes the ribosomal translocon binding site
    • Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I., Beckmann R. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science 2006, 312(5774):745-747.
    • (2006) Science , vol.312 , Issue.5774 , pp. 745-747
    • Halic, M.1    Gartmann, M.2    Schlenker, O.3    Mielke, T.4    Pool, M.R.5    Sinning, I.6    Beckmann, R.7
  • 110
    • 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., Stark H. Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy. Nature 2010, 466(7304):329-333.
    • (2010) Nature , vol.466 , Issue.7304 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Wintermeyer, W.3    Rodnina, M.V.4    Stark, H.5
  • 111
    • 77953625418 scopus 로고    scopus 로고
    • Structure and dynamics of a processive Brownian motor: the translating ribosome
    • Frank J., Gonzalez R.L. Structure and dynamics of a processive Brownian motor: the translating ribosome. Annu. Rev. Biochem. 2010, 79:381-412.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 381-412
    • Frank, J.1    Gonzalez, R.L.2
  • 112
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z., Horwich A.L., Sigler P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388(6644):741-750.
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 113
    • 58149229533 scopus 로고    scopus 로고
    • Chaperonin complex with a newly folded protein encapsulated in the folding chamber
    • Clare D.K., Bakkes P.J., van Heerikhuizen H., van der Vies S.M., Saibil H.R. Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature 2009, 457(7225):107-110.
    • (2009) Nature , vol.457 , Issue.7225 , pp. 107-110
    • Clare, D.K.1    Bakkes, P.J.2    van Heerikhuizen, H.3    van der Vies, S.M.4    Saibil, H.R.5
  • 114
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., Seemuller E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998, 92(3):367-380.
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 116
    • 18744374439 scopus 로고    scopus 로고
    • A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy
    • Rockel B., Peters J., Kuhlmorgen B., Glaeser R.M., Baumeister W. A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy. EMBO J. 2002, 21(22):5979-5984.
    • (2002) EMBO J. , vol.21 , Issue.22 , pp. 5979-5984
    • Rockel, B.1    Peters, J.2    Kuhlmorgen, B.3    Glaeser, R.M.4    Baumeister, W.5
  • 119
    • 48749114826 scopus 로고    scopus 로고
    • Native 3-D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer U.E., Sodeik B., Grunewald K. Native 3-D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc. Natl. Acad. Sci. USA 2008, 105(30):10559-10564.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.30 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grunewald, K.3
  • 120
    • 35148839574 scopus 로고    scopus 로고
    • Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography
    • Sartori A., Gatz R., Beck F., Rigort A., Baumeister W., Plitzko J.M. Correlative microscopy: bridging the gap between fluorescence light microscopy and cryo-electron tomography. J. Struct. Biol. 2007, 160(2):135-145.
    • (2007) J. Struct. Biol. , vol.160 , Issue.2 , pp. 135-145
    • Sartori, A.1    Gatz, R.2    Beck, F.3    Rigort, A.4    Baumeister, W.5    Plitzko, J.M.6
  • 122
    • 33847685630 scopus 로고    scopus 로고
    • Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy
    • Marko M., Hsieh C., Schalek R., Frank J., Mannella C. Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy. Nat. Methods 2007, 4(3):215-217.
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 215-217
    • Marko, M.1    Hsieh, C.2    Schalek, R.3    Frank, J.4    Mannella, C.5
  • 124
    • 29244462551 scopus 로고    scopus 로고
    • Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography
    • Winkler H., Taylor K.A. Accurate marker-free alignment with simultaneous geometry determination and reconstruction of tilt series in electron tomography. Ultramicroscopy 2006, 106(3):240-254.
    • (2006) Ultramicroscopy , vol.106 , Issue.3 , pp. 240-254
    • Winkler, H.1    Taylor, K.A.2
  • 125
    • 0029311291 scopus 로고
    • A marker-free alignment method for electron tomography
    • Liu Y., Penczek P.A., McEwen B.F., Frank J. A marker-free alignment method for electron tomography. Ultramicroscopy 1995, 58(3-4):393-402.
    • (1995) Ultramicroscopy , vol.58 , Issue.3-4 , pp. 393-402
    • Liu, Y.1    Penczek, P.A.2    McEwen, B.F.3    Frank, J.4
  • 127
    • 0035783045 scopus 로고    scopus 로고
    • Automatic alignment of transmission electron microscope tilt series without fiducial markers
    • Brandt S., Heikkonen J., Engelhardt P. Automatic alignment of transmission electron microscope tilt series without fiducial markers. J. Struct. Biol. 2001, 136(3):201-213.
    • (2001) J. Struct. Biol. , vol.136 , Issue.3 , pp. 201-213
    • Brandt, S.1    Heikkonen, J.2    Engelhardt, P.3
  • 128
    • 0002439918 scopus 로고
    • Least-squares method of alignment using markers
    • Plenum Press, New York, J. Frank (Ed.)
    • Lawrence M.C. Least-squares method of alignment using markers. Electron Tomography 1992, 197-204. Plenum Press, New York. J. Frank (Ed.).
    • (1992) Electron Tomography , pp. 197-204
    • Lawrence, M.C.1
  • 129
    • 33646074519 scopus 로고    scopus 로고
    • Tilt-series and electron microscope alignment for the correction of the non-perpendicularity of beam and tilt-axis
    • Diez D.C., Seybert A., Frangakis A.S. Tilt-series and electron microscope alignment for the correction of the non-perpendicularity of beam and tilt-axis. J. Struct. Biol. 2006, 154(2):195-205.
    • (2006) J. Struct. Biol. , vol.154 , Issue.2 , pp. 195-205
    • Diez, D.C.1    Seybert, A.2    Frangakis, A.S.3
  • 130
    • 0037288048 scopus 로고    scopus 로고
    • Rachel, R., Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography
    • Nickell S., Hegerl R., Baumeister W. Rachel, R., Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography. J. Struct. Biol. 2003, 141(1):34-42.
    • (2003) J. Struct. Biol. , vol.141 , Issue.1 , pp. 34-42
    • Nickell, S.1    Hegerl, R.2    Baumeister, W.3
  • 133
    • 0342894782 scopus 로고    scopus 로고
    • Energy filtered electron tomography of ice-embedded actin and vesicles
    • Grimm R., Barmann M., Hackl W., Typke D., Sackmann E., Baumeister W. Energy filtered electron tomography of ice-embedded actin and vesicles. Biophys. J. 1997, 72(1):482-489.
    • (1997) Biophys. J. , vol.72 , Issue.1 , pp. 482-489
    • Grimm, R.1    Barmann, M.2    Hackl, W.3    Typke, D.4    Sackmann, E.5    Baumeister, W.6
  • 134
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O., Weber I., Frangakis A.S., Nicastro D., Gerisch G., Baumeister W. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 2002, 298(5596):1209-1213.
    • (2002) Science , vol.298 , Issue.5596 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 136
    • 2942544494 scopus 로고    scopus 로고
    • Computational exploration of structural information from cryo-electron tomograms
    • Frangakis A.S., Forster F. Computational exploration of structural information from cryo-electron tomograms. Curr. Opin. Struct. Biol. 2004, 14(3):325-331.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , Issue.3 , pp. 325-331
    • Frangakis, A.S.1    Forster, F.2
  • 137
    • 0344983355 scopus 로고    scopus 로고
    • Applications of a bilateral denoising filter in biological electron microscopy
    • Jiang W., Baker M.L., Wu Q., Bajaj C., Chiu W. Applications of a bilateral denoising filter in biological electron microscopy. J. Struct. Biol. 2003, 144(1-2):114-122.
    • (2003) J. Struct. Biol. , vol.144 , Issue.1-2 , pp. 114-122
    • Jiang, W.1    Baker, M.L.2    Wu, Q.3    Bajaj, C.4    Chiu, W.5
  • 138
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis A.S., Hegerl R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 2001, 135(3):239-250.
    • (2001) J. Struct. Biol. , vol.135 , Issue.3 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 139
    • 0035083779 scopus 로고    scopus 로고
    • Wavelet transform filtering and nonlinear anisotropic diffusion assessed for signal reconstruction performance on multidimensional biomedical data
    • Frangakis A.S., Stoschek A., Hegerl R. Wavelet transform filtering and nonlinear anisotropic diffusion assessed for signal reconstruction performance on multidimensional biomedical data. IEEE Transactions on Biomedical Engineering 2001, 48(2):213-222.
    • (2001) IEEE Transactions on Biomedical Engineering , vol.48 , Issue.2 , pp. 213-222
    • Frangakis, A.S.1    Stoschek, A.2    Hegerl, R.3
  • 140
    • 0345414562 scopus 로고    scopus 로고
    • An improved algorithm for anisotropic nonlinear diffusion for denoising cryo-tomograms
    • Fernandez J.J., Li S. An improved algorithm for anisotropic nonlinear diffusion for denoising cryo-tomograms. J. Struct. Biol. 2003, 144(1-2):152-161.
    • (2003) J. Struct. Biol. , vol.144 , Issue.1-2 , pp. 152-161
    • Fernandez, J.J.1    Li, S.2
  • 141
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J.R., Mastronarde D.N., McIntosh J.R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 1996, 116(1):71-76.
    • (1996) J. Struct. Biol. , vol.116 , Issue.1 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 142
    • 0036417303 scopus 로고    scopus 로고
    • Segmentation of two- and three-dimensional data from electron microscopy using eigenvector analysis
    • Frangakis A.S., Hegerl R. Segmentation of two- and three-dimensional data from electron microscopy using eigenvector analysis. J. Struct. Biol. 2002, 138:105-113.
    • (2002) J. Struct. Biol. , vol.138 , pp. 105-113
    • Frangakis, A.S.1    Hegerl, R.2
  • 143
    • 0036424944 scopus 로고    scopus 로고
    • A novel three-dimensional variant of the watershed transform for segmentation of electron density maps
    • Volkmann N. A novel three-dimensional variant of the watershed transform for segmentation of electron density maps. J. Struct. Biol. 2002, 138(1-2):123-129.
    • (2002) J. Struct. Biol. , vol.138 , Issue.1-2 , pp. 123-129
    • Volkmann, N.1
  • 145
    • 14844324485 scopus 로고    scopus 로고
    • Morphological characterization of molecular complexes present in the synaptic cleft
    • Lucic V., Yang T., Schweikert G., Förster F., Baumeister W. Morphological characterization of molecular complexes present in the synaptic cleft. Structure (Camb) 2005, 13(3):423-434.
    • (2005) Structure (Camb) , vol.13 , Issue.3 , pp. 423-434
    • Lucic, V.1    Yang, T.2    Schweikert, G.3    Förster, F.4    Baumeister, W.5
  • 146
    • 0034687769 scopus 로고    scopus 로고
    • Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms
    • Böhm J., Frangakis A.S., Hegerl R., Nickell S., Typke D., Baumeister W. Toward detecting and identifying macromolecules in a cellular context: template matching applied to electron tomograms. Proc. Natl. Acad. Sci. USA 2000, 97(26):14245-14250.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.26 , pp. 14245-14250
    • Böhm, J.1    Frangakis, A.S.2    Hegerl, R.3    Nickell, S.4    Typke, D.5    Baumeister, W.6
  • 148
    • 33750527990 scopus 로고    scopus 로고
    • Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition
    • Ortiz J.O., Förster F., Kurner J., Linaroudis A.A., Baumeister W. Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition. J. Struct. Biol. 2006, 156(2):334-341.
    • (2006) J. Struct. Biol. , vol.156 , Issue.2 , pp. 334-341
    • Ortiz, J.O.1    Förster, F.2    Kurner, J.3    Linaroudis, A.A.4    Baumeister, W.5
  • 149
    • 68449102172 scopus 로고    scopus 로고
    • Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans
    • Malmstrom J., Beck M., Schmidt A., Lange V., Deutsch E.W., Aebersold R. Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans. Nature 2009, 460(7256):762-765.
    • (2009) Nature , vol.460 , Issue.7256 , pp. 762-765
    • Malmstrom, J.1    Beck, M.2    Schmidt, A.3    Lange, V.4    Deutsch, E.W.5    Aebersold, R.6
  • 152
    • 77956006893 scopus 로고    scopus 로고
    • The three-dimensional organization of polyribosomes in intact human cells
    • Brandt F., Carlson L.A., Hartl F.U., Baumeister W., Grunewald K. The three-dimensional organization of polyribosomes in intact human cells. Mol. Cell 2010, 39(4):560-569.
    • (2010) Mol. Cell , vol.39 , Issue.4 , pp. 560-569
    • Brandt, F.1    Carlson, L.A.2    Hartl, F.U.3    Baumeister, W.4    Grunewald, K.5
  • 153
    • 0020536972 scopus 로고
    • Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs
    • Oettl H., Hegerl R., Hoppe W. Three-dimensional reconstruction and averaging of 50 S ribosomal subunits of Escherichia coli from electron micrographs. J. Mol. Biol. 1983, 163(3):431-450.
    • (1983) J. Mol. Biol. , vol.163 , Issue.3 , pp. 431-450
    • Oettl, H.1    Hegerl, R.2    Hoppe, W.3
  • 154
    • 0020633272 scopus 로고
    • Three-dimensional reconstruction and averaging of 30 S ribosomal subunits of Escherichia coli from electron micrographs
    • Knauer V., Hegerl R., Hoppe W. Three-dimensional reconstruction and averaging of 30 S ribosomal subunits of Escherichia coli from electron micrographs. J. Mol. Biol. 1983, 163(3):409-430.
    • (1983) J. Mol. Biol. , vol.163 , Issue.3 , pp. 409-430
    • Knauer, V.1    Hegerl, R.2    Hoppe, W.3
  • 155
    • 3943108224 scopus 로고
    • Influence of electron noise on three-dimensional image reconstruction
    • Hegerl R., Hoppe W. Influence of electron noise on three-dimensional image reconstruction. Z. Naturforschung 1976, 31a:1717-1721.
    • (1976) Z. Naturforschung , vol.31 a , pp. 1717-1721
    • Hegerl, R.1    Hoppe, W.2
  • 156
    • 0029379689 scopus 로고
    • The relevance of dose-fractionation in tomography of radiation-sensitive specimens
    • McEwen B.F., Downing K.H., Glaeser R.M. The relevance of dose-fractionation in tomography of radiation-sensitive specimens. Ultramicroscopy 1995, 60:357-373.
    • (1995) Ultramicroscopy , vol.60 , pp. 357-373
    • McEwen, B.F.1    Downing, K.H.2    Glaeser, R.M.3
  • 157
    • 0019662987 scopus 로고
    • Some remarks concerning the influence of electron noise on 3-D reconstruction
    • Hoppe W., Hegerl R. Some remarks concerning the influence of electron noise on 3-D reconstruction. Ultramicroscopy 1981, 6(2):205-206.
    • (1981) Ultramicroscopy , vol.6 , Issue.2 , pp. 205-206
    • Hoppe, W.1    Hegerl, R.2
  • 158
    • 33847232164 scopus 로고    scopus 로고
    • Structure determination in situ by averaging of tomograms
    • Förster F., Hegerl R. Structure determination in situ by averaging of tomograms. Methods Cell. Biol. 2007, 79:741-767.
    • (2007) Methods Cell. Biol. , vol.79 , pp. 741-767
    • Förster, F.1    Hegerl, R.2
  • 159
    • 69249115197 scopus 로고    scopus 로고
    • Membrane protein structure determination using cryo-electron tomography and 3-D image averaging
    • Bartesaghi A., Subramaniam S. Membrane protein structure determination using cryo-electron tomography and 3-D image averaging. Curr. Opin. Struct. Biol. 2009, 19(4):402-407.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , Issue.4 , pp. 402-407
    • Bartesaghi, A.1    Subramaniam, S.2
  • 161
    • 44449179947 scopus 로고    scopus 로고
    • Classification and 3-D averaging with missing wedge correction in biological electron tomography
    • Bartesaghi A., Sprechmann P., Liu J., Randall G., Sapiro G., Subramaniam S. Classification and 3-D averaging with missing wedge correction in biological electron tomography. J. Struct. Biol. 2008, 162(3):436-450.
    • (2008) J. Struct. Biol. , vol.162 , Issue.3 , pp. 436-450
    • Bartesaghi, A.1    Sprechmann, P.2    Liu, J.3    Randall, G.4    Sapiro, G.5    Subramaniam, S.6
  • 163
    • 40649109028 scopus 로고    scopus 로고
    • Methods for aligning and for averaging 3-D volumes with missing data
    • Schmid M.F., Booth C.R. Methods for aligning and for averaging 3-D volumes with missing data. J. Struct. Biol. 2008, 161(3):243-248.
    • (2008) J. Struct. Biol. , vol.161 , Issue.3 , pp. 243-248
    • Schmid, M.F.1    Booth, C.R.2
  • 164
    • 58349085125 scopus 로고    scopus 로고
    • Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes
    • Winkler H., Zhu P., Liu J., Ye F., Roux K.H., Taylor K.A. Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes. J. Struct. Biol. 2009, 165(2):64-77.
    • (2009) J. Struct. Biol. , vol.165 , Issue.2 , pp. 64-77
    • Winkler, H.1    Zhu, P.2    Liu, J.3    Ye, F.4    Roux, K.H.5    Taylor, K.A.6
  • 165
    • 40649128324 scopus 로고    scopus 로고
    • Classification of cryo-electron sub-tomograms using constrained correlation
    • Förster F., Pruggnaller S., Seybert A., Frangakis A.S. Classification of cryo-electron sub-tomograms using constrained correlation. J. Struct. Biol. 2008, 161(3):276-286.
    • (2008) J. Struct. Biol. , vol.161 , Issue.3 , pp. 276-286
    • Förster, F.1    Pruggnaller, S.2    Seybert, A.3    Frangakis, A.S.4
  • 166
    • 33845310367 scopus 로고    scopus 로고
    • 3-D reconstruction and processing of volumetric data in cryo-electron tomography
    • Epub 2006 Aug 11
    • Winkler H. 3-D reconstruction and processing of volumetric data in cryo-electron tomography. J. Struct. Biol. 2007, 157(1):126-137. Epub 2006 Aug 11.
    • (2007) J. Struct. Biol. , vol.157 , Issue.1 , pp. 126-137
    • Winkler, H.1
  • 167
  • 169
    • 33748038359 scopus 로고    scopus 로고
    • Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ
    • Zanetti G., Briggs J.A., Grunewald K., Sattentau Q.J., Fuller S.D. Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathog. 2006, 2(8):e83.
    • (2006) PLoS Pathog. , vol.2 , Issue.8
    • Zanetti, G.1    Briggs, J.A.2    Grunewald, K.3    Sattentau, Q.J.4    Fuller, S.D.5
  • 170
  • 172
    • 77953613557 scopus 로고    scopus 로고
    • Probabilistic principal component analysis with expectation maximization (PPCA-EM) facilitates volume classification and estimates the missing data
    • Yu L., Snapp R.R., Ruiz T., Radermacher M. Probabilistic principal component analysis with expectation maximization (PPCA-EM) facilitates volume classification and estimates the missing data. J. Struct. Biol. 2010.
    • (2010) J. Struct. Biol.
    • Yu, L.1    Snapp, R.R.2    Ruiz, T.3    Radermacher, M.4
  • 173
    • 71049139404 scopus 로고    scopus 로고
    • Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization
    • Scheres S.H., Melero R., Valle M., Carazo J.M. Averaging of electron subtomograms and random conical tilt reconstructions through likelihood optimization. Structure 2009, 17(12):1563-1572.
    • (2009) Structure , vol.17 , Issue.12 , pp. 1563-1572
    • Scheres, S.H.1    Melero, R.2    Valle, M.3    Carazo, J.M.4
  • 175
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Förster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449(7162):611-615.
    • (2007) Nature , vol.449 , Issue.7162 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Förster, F.3    Baumeister, W.4    Medalia, O.5
  • 177
    • 51349162563 scopus 로고    scopus 로고
    • Molecular architecture of native HIV-1 gp120 trimers
    • Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S. Molecular architecture of native HIV-1 gp120 trimers. Nature 2008, 455(7209):109-113.
    • (2008) Nature , vol.455 , Issue.7209 , pp. 109-113
    • Liu, J.1    Bartesaghi, A.2    Borgnia, M.J.3    Sapiro, G.4    Subramaniam, S.5
  • 178
    • 33748295677 scopus 로고    scopus 로고
    • In situ structure of the complete Treponema primitia flagellar motor
    • Murphy G.E., Leadbetter J.R., Jensen G.J. In situ structure of the complete Treponema primitia flagellar motor. Nature 2006, 442(7106):1062-1064.
    • (2006) Nature , vol.442 , Issue.7106 , pp. 1062-1064
    • Murphy, G.E.1    Leadbetter, J.R.2    Jensen, G.J.3
  • 180
    • 27644477833 scopus 로고    scopus 로고
    • 3-D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    • Nicastro D., McIntosh J.R., Baumeister W. 3-D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography. Proc. Natl. Acad. Sci. USA 2005, 102(44):15889-15894.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.44 , pp. 15889-15894
    • Nicastro, D.1    McIntosh, J.R.2    Baumeister, W.3
  • 181
    • 33747598723 scopus 로고    scopus 로고
    • The molecular architecture of axonemes revealed by cryoelectron tomography
    • Nicastro D., Schwartz C., Pierson J., Gaudette R., Porter M.E., McIntosh J.R. The molecular architecture of axonemes revealed by cryoelectron tomography. Science 2006, 313(5789):944-948.
    • (2006) Science , vol.313 , Issue.5789 , pp. 944-948
    • Nicastro, D.1    Schwartz, C.2    Pierson, J.3    Gaudette, R.4    Porter, M.E.5    McIntosh, J.R.6
  • 182
    • 74049111826 scopus 로고    scopus 로고
    • The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella
    • Heuser T., Raytchev M., Krell J., Porter M.E., Nicastro D. The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella. J. Cell. Biol. 2009, 187(6):921-933.
    • (2009) J. Cell. Biol. , vol.187 , Issue.6 , pp. 921-933
    • Heuser, T.1    Raytchev, M.2    Krell, J.3    Porter, M.E.4    Nicastro, D.5
  • 183
    • 77953259866 scopus 로고    scopus 로고
    • Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis
    • Movassagh T., Bui K.H., Sakakibara H., Oiwa K., Ishikawa T. Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis. Nat. Struct. Mol. Biol. 2010, 17(6):761-767.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.6 , pp. 761-767
    • Movassagh, T.1    Bui, K.H.2    Sakakibara, H.3    Oiwa, K.4    Ishikawa, T.5
  • 185
    • 0024278917 scopus 로고
    • Images of purple membrane at 2.8 A resolution obtained by cryo-electron microscopy
    • Baldwin J.M., Henderson R., Beckman E., Zemlin F. Images of purple membrane at 2.8 A resolution obtained by cryo-electron microscopy. J. Mol. Biol. 1988, 202(3):585-591.
    • (1988) J. Mol. Biol. , vol.202 , Issue.3 , pp. 585-591
    • Baldwin, J.M.1    Henderson, R.2    Beckman, E.3    Zemlin, F.4
  • 186
    • 67650282016 scopus 로고    scopus 로고
    • Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
    • Raunser S., Walz T. Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment. Annu. Rev. Biophys. 2009, 38:89-105.
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 89-105
    • Raunser, S.1    Walz, T.2
  • 187
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 A resolution
    • Lowe J., Li H., Downing K.H., Nogales E. Refined structure of alpha beta-tubulin at 3.5 A resolution. J. Mol. Biol. 2001, 313(5):1045-1057.
    • (2001) J. Mol. Biol. , vol.313 , Issue.5 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 188
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • Gonen T., Cheng Y., Sliz P., Hiroaki Y., Fujiyoshi Y., Harrison S.C., Walz T. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 2005, 438(7068):633-638.
    • (2005) Nature , vol.438 , Issue.7068 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 189
    • 0024335508 scopus 로고
    • Dynamic focussing for recording images from tilted samples in small-spot scanning with a transmission electron microscope
    • Zemlin F. Dynamic focussing for recording images from tilted samples in small-spot scanning with a transmission electron microscope. J. Electron. Microsc. Tech. 1989, 11(4):251-257.
    • (1989) J. Electron. Microsc. Tech. , vol.11 , Issue.4 , pp. 251-257
    • Zemlin, F.1
  • 190
    • 0026499524 scopus 로고
    • Automatic focus correction for spot-scan imaging of tilted specimens
    • Downing K.H. Automatic focus correction for spot-scan imaging of tilted specimens. Ultramicroscopy 1992, 46(1-4):199-206.
    • (1992) Ultramicroscopy , vol.46 , Issue.1-4 , pp. 199-206
    • Downing, K.H.1
  • 191
    • 84882802347 scopus 로고
    • In 3-D Reconstruction of Single Particles by Quasi-conical Tilting from Micrographs Recorded with Dynamic Focusing, 12th Int. Congr. on Electron Microscopy, Seattle, 1990; Seattle
    • Typke, D.; Pfeifer, G.; Hegerl, R.; Baumeister, W. In 3-D Reconstruction of Single Particles by Quasi-conical Tilting from Micrographs Recorded with Dynamic Focusing, 12th Int. Congr. on Electron Microscopy, Seattle, 1990; Seattle, 1990.
    • (1990)
    • Typke, D.1    Pfeifer, G.2    Hegerl, R.3    Baumeister, W.4
  • 192
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 1990, 213(4):899-929.
    • (1990) J. Mol. Biol. , vol.213 , Issue.4 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 193
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff N., Ceska T.A., Downing K.H., Baldwin J.M., Henderson R. Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 1996, 259(3):393-421.
    • (1996) J. Mol. Biol. , vol.259 , Issue.3 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 196
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H., Han B.-G., Lee J.K., Walian P., Jap B.K. Structural basis of water-specific transport through the AQP1 water channel. Nature 2001, 414(6866):872-878.
    • (2001) Nature , vol.414 , Issue.6866 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 197
    • 0035861454 scopus 로고    scopus 로고
    • Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF
    • de Groot B.L., Grubmuller H. Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF. Science 2001, 294(5550):2353-2357.
    • (2001) Science , vol.294 , Issue.5550 , pp. 2353-2357
    • de Groot, B.L.1    Grubmuller, H.2
  • 198
    • 0035979666 scopus 로고    scopus 로고
    • Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer
    • Zhu F., Tajkhorshid E., Schulten K. Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer. FEBS Lett. 2001, 504(3):212-218.
    • (2001) FEBS Lett. , vol.504 , Issue.3 , pp. 212-218
    • Zhu, F.1    Tajkhorshid, E.2    Schulten, K.3
  • 200
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 2005, 346(4):967-989.
    • (2005) J. Mol. Biol. , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 201
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 1998, 391(6663):199-203.
    • (1998) Nature , vol.391 , Issue.6663 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 204
    • 27344449197 scopus 로고    scopus 로고
    • Progress in modeling of protein structures and interactions
    • Schueler-Furman O., Wang C., Bradley P., Misura K., Baker D. Progress in modeling of protein structures and interactions. Science 2005, 310(5748):638-642.
    • (2005) Science , vol.310 , Issue.5748 , pp. 638-642
    • Schueler-Furman, O.1    Wang, C.2    Bradley, P.3    Misura, K.4    Baker, D.5
  • 206
    • 65349171739 scopus 로고    scopus 로고
    • Comparative Modeling of Drug Target Proteins
    • Elsevier, Oxford, J. Taylor, D. Triggle (Eds.)
    • Eswar N., Sali A. Comparative Modeling of Drug Target Proteins. Computer-Assisted Drug Design 2007, 215-236. Elsevier, Oxford. J. Taylor, D. Triggle (Eds.).
    • (2007) Computer-Assisted Drug Design , pp. 215-236
    • Eswar, N.1    Sali, A.2
  • 207
    • 0032568596 scopus 로고    scopus 로고
    • Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships
    • Brenner S.E., Chothia C., Hubbard T.J. Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships. Proc. Natl. Acad. Sci. USA 1998, 95(11):6073-6078.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.11 , pp. 6073-6078
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.3
  • 208
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J., Blundell T.L., Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol. 2001, 310(1):243-257.
    • (2001) J. Mol. Biol. , vol.310 , Issue.1 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 209
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences
    • Jones D.T. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 1999, 287(4):797-815.
    • (1999) J. Mol. Biol. , vol.287 , Issue.4 , pp. 797-815
    • Jones, D.T.1
  • 210
    • 12844256969 scopus 로고    scopus 로고
    • Structural characterization of components of protein assemblies by comparative modeling and electron cryo-microscopy
    • Topf M., Baker M.L., John B., Chiu W., Sali A. Structural characterization of components of protein assemblies by comparative modeling and electron cryo-microscopy. J. Struct. Biol. 2005, 149(2):191-203.
    • (2005) J. Struct. Biol. , vol.149 , Issue.2 , pp. 191-203
    • Topf, M.1    Baker, M.L.2    John, B.3    Chiu, W.4    Sali, A.5
  • 212
    • 0034802465 scopus 로고    scopus 로고
    • Modeling tricks and fitting techniques for multiresolution structures
    • Wriggers W., Chácon P. Modeling tricks and fitting techniques for multiresolution structures. Structure 2001, 9:779-788.
    • (2001) Structure , vol.9 , pp. 779-788
    • Wriggers, W.1    Chácon, P.2
  • 213
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • Volkmann N., Hanein D. Quantitative fitting of atomic models into observed densities derived by electron microscopy. J. Struct. Biol. 1999, 125(2-3):176-184.
    • (1999) J. Struct. Biol. , vol.125 , Issue.2-3 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 214
    • 0032780181 scopus 로고    scopus 로고
    • Situs: a package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 1999, 125(2-3):185-195.
    • (1999) J. Struct. Biol. , vol.125 , Issue.2-3 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 215
    • 0035906702 scopus 로고    scopus 로고
    • Bridging the information gap: computational tools for intermediate resolution structure interpretation
    • Jiang W., Baker M.L., Ludtke S.J., Chiu W. Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 2001, 308(5):1033-1044.
    • (2001) J. Mol. Biol. , vol.308 , Issue.5 , pp. 1033-1044
    • Jiang, W.1    Baker, M.L.2    Ludtke, S.J.3    Chiu, W.4
  • 216
    • 33748351384 scopus 로고    scopus 로고
    • NORMA: a tool for flexible fitting of high-resolution protein structures into low-resolution electron-microscopy-derived density maps
    • Suhre K., Navaza J., Sanejouand Y.H. NORMA: a tool for flexible fitting of high-resolution protein structures into low-resolution electron-microscopy-derived density maps. Acta. Crystallogr. D Biol. Crystallogr. 2006, 62(Pt 9):1098-1100.
    • (2006) Acta. Crystallogr. D Biol. Crystallogr. , vol.62 , Issue.PT 9 , pp. 1098-1100
    • Suhre, K.1    Navaza, J.2    Sanejouand, Y.H.3
  • 217
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard T.D., Huang C.C., Ferrin T.E. Visualizing density maps with UCSF Chimera. J Struct. Biol. 2007, 157(1):281-287.
    • (2007) J Struct. Biol. , vol.157 , Issue.1 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 218
    • 14844311200 scopus 로고    scopus 로고
    • Fitting of high-resolution structures into electron microscopy reconstruction images
    • Fabiola F., Chapman M.S. Fitting of high-resolution structures into electron microscopy reconstruction images. Structure 2005, 13(3):389-400.
    • (2005) Structure , vol.13 , Issue.3 , pp. 389-400
    • Fabiola, F.1    Chapman, M.S.2
  • 219
    • 0033776245 scopus 로고    scopus 로고
    • Docking structures of domains into maps from cryo-electron microscopy using local correlation
    • Roseman A.M. Docking structures of domains into maps from cryo-electron microscopy using local correlation. Acta Crystallographica D 2000, 56:1332-1340.
    • (2000) Acta Crystallographica D , vol.56 , pp. 1332-1340
    • Roseman, A.M.1
  • 221
    • 58149293674 scopus 로고    scopus 로고
    • Multiple subunit fitting into a low-resolution density map of a macromolecular complex using a gaussian mixture model
    • Kawabata T. Multiple subunit fitting into a low-resolution density map of a macromolecular complex using a gaussian mixture model. Biophys. J. 2008, 95(10):4643-4658.
    • (2008) Biophys. J. , vol.95 , Issue.10 , pp. 4643-4658
    • Kawabata, T.1
  • 222
    • 63449125993 scopus 로고    scopus 로고
    • Inferential optimization for simultaneous fitting of multiple components into a CryoEM map of their assembly
    • Lasker K., Topf M., Sali A., Wolfson H.J. Inferential optimization for simultaneous fitting of multiple components into a CryoEM map of their assembly. J. Mol. Biol. 2009, 388(1):180-194.
    • (2009) J. Mol. Biol. , vol.388 , Issue.1 , pp. 180-194
    • Lasker, K.1    Topf, M.2    Sali, A.3    Wolfson, H.J.4
  • 223
    • 77954209615 scopus 로고    scopus 로고
    • A fast mathematical programming procedure for simultaneous fitting of assembly components into cryoEM density maps
    • Zhang S., Vasishtan D., Xu M., Topf M., Alber F. A fast mathematical programming procedure for simultaneous fitting of assembly components into cryoEM density maps. Bioinformatics 2010, 26(12):i261-i268.
    • (2010) Bioinformatics , vol.26 , Issue.12
    • Zhang, S.1    Vasishtan, D.2    Xu, M.3    Topf, M.4    Alber, F.5
  • 224
    • 0026021882 scopus 로고
    • Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product
    • Kaelin W.G., Pallas D.C., DeCaprio J.A., Kaye F.J., Livingston D.M. Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product. Cell 1991, 64(3):521-532.
    • (1991) Cell , vol.64 , Issue.3 , pp. 521-532
    • Kaelin, W.G.1    Pallas, D.C.2    DeCaprio, J.A.3    Kaye, F.J.4    Livingston, D.M.5
  • 225
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 2003, 38(12):1225-1237.
    • (2003) J. Mass Spectrom. , vol.38 , Issue.12 , pp. 1225-1237
    • Sinz, A.1
  • 226
    • 34548426979 scopus 로고    scopus 로고
    • The role of mass spectrometry in structure elucidation of dynamic protein complexes
    • Sharon M., Robinson C.V. The role of mass spectrometry in structure elucidation of dynamic protein complexes. Annu. Rev. Biochem. 2007, 76:167-193.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 167-193
    • Sharon, M.1    Robinson, C.V.2
  • 228
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • Alber F., Forster F., Korkin D., Topf M., Sali A. Integrating diverse data for structure determination of macromolecular assemblies. Annu. Rev. Biochem. 2008, 77:443-477.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 443-477
    • Alber, F.1    Forster, F.2    Korkin, D.3    Topf, M.4    Sali, A.5
  • 232
    • 77951945222 scopus 로고    scopus 로고
    • Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly
    • Tomko R.J., Funakoshi M., Schneider K., Wang J., Hochstrasser M. Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly. Mol. Cell 2010, 38(3):393-403.
    • (2010) Mol. Cell , vol.38 , Issue.3 , pp. 393-403
    • Tomko, R.J.1    Funakoshi, M.2    Schneider, K.3    Wang, J.4    Hochstrasser, M.5
  • 233
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brunger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science 1987, 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 235
    • 0001832403 scopus 로고
    • Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron-density function
    • Chapman M. Restrained real-space macromolecular atomic refinement using a new resolution-dependent electron-density function. Acta Crystallogr. A 1995, 51:69-80.
    • (1995) Acta Crystallogr. A , vol.51 , pp. 69-80
    • Chapman, M.1
  • 236
    • 0344120716 scopus 로고    scopus 로고
    • Low-resolution structure refinement in electron microscopy
    • Chen J.Z., Fürst J., Chapman M.S., Grigorieff N. Low-resolution structure refinement in electron microscopy. J. Struct. Biol. 2003, 144(1-2):144-151.
    • (2003) J. Struct. Biol. , vol.144 , Issue.1-2 , pp. 144-151
    • Chen, J.Z.1    Fürst, J.2    Chapman, M.S.3    Grigorieff, N.4
  • 237
    • 0033863336 scopus 로고    scopus 로고
    • Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures
    • Wriggers W., Agrawal R.K., Drew D.L., McCammon A., Frank J. Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures. Biophys. J. 2000, 79(3):1670-1678.
    • (2000) Biophys. J. , vol.79 , Issue.3 , pp. 1670-1678
    • Wriggers, W.1    Agrawal, R.K.2    Drew, D.L.3    McCammon, A.4    Frank, J.5
  • 238
    • 0035783173 scopus 로고    scopus 로고
    • Using situs for flexible and rigid-body fitting of multiresolution single-molecule data
    • Wriggers W., Birmanns S. Using situs for flexible and rigid-body fitting of multiresolution single-molecule data. J. Struct. Biol. 2001, 133(2-3):193-202.
    • (2001) J. Struct. Biol. , vol.133 , Issue.2-3 , pp. 193-202
    • Wriggers, W.1    Birmanns, S.2
  • 239
    • 4344716056 scopus 로고    scopus 로고
    • Normal mode based flexible fitting of high-resolution structure into low-resolution experimental data from cryo-EM
    • Tama F., Miyashita O., Brooks C.L. Normal mode based flexible fitting of high-resolution structure into low-resolution experimental data from cryo-EM. Journal of Structural Biology 2004, 147(3):315-326.
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 315-326
    • Tama, F.1    Miyashita, O.2    Brooks, C.L.3
  • 241
    • 38949092920 scopus 로고    scopus 로고
    • Protein structure fitting and refinement guided by cryo-EM density
    • Topf M., Lasker K., Webb B., Wolfson H., Chiu W., Sali A. Protein structure fitting and refinement guided by cryo-EM density. Structure 2008, 16(2):295-307.
    • (2008) Structure , vol.16 , Issue.2 , pp. 295-307
    • Topf, M.1    Lasker, K.2    Webb, B.3    Wolfson, H.4    Chiu, W.5    Sali, A.6
  • 242
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco L.G., Villa E., Mitra K., Frank J., Schulten K. Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 2008, 16(5):673-683.
    • (2008) Structure , vol.16 , Issue.5 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 243
    • 36749078686 scopus 로고    scopus 로고
    • Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution
    • Schroder G.F., Brunger A.T., Levitt M. Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution. Structure 2007, 15(12):1630-1641.
    • (2007) Structure , vol.15 , Issue.12 , pp. 1630-1641
    • Schroder, G.F.1    Brunger, A.T.2    Levitt, M.3
  • 244
    • 46749096676 scopus 로고    scopus 로고
    • YUP.SCX: coaxing atomic models into medium resolution electron density maps
    • Tan R.K., Devkota B., Harvey S.C. YUP.SCX: coaxing atomic models into medium resolution electron density maps. J. Struct. Biol. 2008, 163(2):163-174.
    • (2008) J. Struct. Biol. , vol.163 , Issue.2 , pp. 163-174
    • Tan, R.K.1    Devkota, B.2    Harvey, S.C.3
  • 246
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • Schroder G.F., Levitt M., Brunger A.T. Super-resolution biomolecular crystallography with low-resolution data. Nature 2010, 464(7292):1218-1222.
    • (2010) Nature , vol.464 , Issue.7292 , pp. 1218-1222
    • Schroder, G.F.1    Levitt, M.2    Brunger, A.T.3
  • 247
    • 41449099769 scopus 로고    scopus 로고
    • Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulations
    • Jolley C.C., Wells S.A., Fromme P., Thorpe M.F. Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulations. Biophys. J. 2008, 94(5):1613-1621.
    • (2008) Biophys. J. , vol.94 , Issue.5 , pp. 1613-1621
    • Jolley, C.C.1    Wells, S.A.2    Fromme, P.3    Thorpe, M.F.4
  • 248
    • 55949095660 scopus 로고    scopus 로고
    • Damped-dynamics flexible fitting
    • Kovacs J.A., Yeager M., Abagyan R. Damped-dynamics flexible fitting. Biophys. J. 2008, 95(7):3192-3207.
    • (2008) Biophys. J. , vol.95 , Issue.7 , pp. 3192-3207
    • Kovacs, J.A.1    Yeager, M.2    Abagyan, R.3
  • 250
    • 4644273133 scopus 로고    scopus 로고
    • An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data
    • Epub 2004 Aug 31
    • Fleishman S.J., Harrington S., Friesner R.A., Honig B., Ben-Tal N. An automatic method for predicting transmembrane protein structures using cryo-EM and evolutionary data. Biophys J. 2004, 87(5):3448-3459. Epub 2004 Aug 31.
    • (2004) Biophys J. , vol.87 , Issue.5 , pp. 3448-3459
    • Fleishman, S.J.1    Harrington, S.2    Friesner, R.A.3    Honig, B.4    Ben-Tal, N.5
  • 251
    • 4644228547 scopus 로고    scopus 로고
    • A Calpha model for the transmembrane alpha helices of gap junction intercellular channels
    • Fleishman S.J., Unger V.M., Yeager M., Ben-Tal N. A Calpha model for the transmembrane alpha helices of gap junction intercellular channels. Mol. Cell 2004, 15(6):879-888.
    • (2004) Mol. Cell , vol.15 , Issue.6 , pp. 879-888
    • Fleishman, S.J.1    Unger, V.M.2    Yeager, M.3    Ben-Tal, N.4
  • 252
    • 68949187842 scopus 로고    scopus 로고
    • Refinement of protein structures into low-resolution density maps using rosetta
    • DiMaio F., Tyka M.D., Baker M.L., Chiu W., Baker D. Refinement of protein structures into low-resolution density maps using rosetta. J. Mol. Biol 2009, 392:181-190.
    • (2009) J. Mol. Biol , vol.392 , pp. 181-190
    • DiMaio, F.1    Tyka, M.D.2    Baker, M.L.3    Chiu, W.4    Baker, D.5


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