메뉴 건너뛰기




Volumn 2013, Issue 2, 2013, Pages

Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ARTICLE; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; IMAGE PROCESSING; IRRADIATION; MACROMOLECULE; NONHUMAN; PROTEIN STRUCTURE; RIBOSOME; RIBOSOME SUBUNIT; SACCHAROMYCES CEREVISIAE; THERMUS THERMOPHILUS; METABOLISM; PROCEDURES; ULTRASTRUCTURE;

EID: 84878580683     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.00461     Document Type: Article
Times cited : (354)

References (32)
  • 1
    • 78650546283 scopus 로고    scopus 로고
    • Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution
    • doi: 10.1073/pnas.1009999107
    • Armache J-P, Jarasch A, Anger AM, Villa E, Becker T, Bhushan S, et al. 2010. Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution. Proc Natl Acad Sci USA 107:19748-53. doi: 10.1073/pnas.1009999107.
    • (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
  • 2
    • 77957222044 scopus 로고    scopus 로고
    • Radiation damage in electron cryomicroscopy
    • doi: 10.1016/S0076-6879(10)81015-8
    • Baker LA, Rubinstein JL. 2010. Radiation damage in electron cryomicroscopy. Methods Enzymol 481:371-88. doi: 10.1016/S0076-6879(10)81015-8.
    • (2010) Methods Enzymol , vol.481 , pp. 371-388
    • Baker, L.A.1    Rubinstein, J.L.2
  • 4
    • 84862783740 scopus 로고    scopus 로고
    • Beam-induced motion of vitrified specimen on holey carbon film
    • doi: 10.1016/j.jsb.2012.02.003
    • Brilot AF, Chen JZ, Cheng A, Pan J, Harrison SC, Potter CS, et al. 2012. Beam-induced motion of vitrified specimen on holey carbon film. J Struct Biol 177:630-7. doi: 10.1016/j.jsb.2012.02.003.
    • (2012) J Struct Biol , vol.177 , pp. 630-637
    • Brilot, A.F.1    Chen, J.Z.2    Cheng, A.3    Pan, J.4    Harrison, S.C.5    Potter, C.S.6
  • 5
    • 84868573207 scopus 로고    scopus 로고
    • Movies of ice-embedded particles enhance resolution in electron cryo-microscopy
    • doi: 10.1016/j.str.2012.08.026
    • Campbell MG, Cheng A, Brilot AF, Moeller A, Lyumkis D, Veesler D, et al. 2012. Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. Structure 20:1823-8. doi: 10.1016/j.str.2012.08.026.
    • (2012) Structure , vol.20 , pp. 1823-1828
    • Campbell, M.G.1    Cheng, A.2    Brilot, A.F.3    Moeller, A.4    Lyumkis, D.5    Veesler, D.6
  • 6
    • 77954650144 scopus 로고    scopus 로고
    • Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy
    • doi: 10.1038/nature09206
    • Fischer N, Konevega AL, Wintermeyer W, Rodnina MV, Stark H. 2010. Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopy. Nature 466:329-33. doi: 10.1038/nature09206.
    • (2010) Nature , vol.466 , pp. 329-333
    • Fischer, N.1    Konevega, A.L.2    Wintermeyer, W.3    Rodnina, M.V.4    Stark, H.5
  • 7
    • 0026045381 scopus 로고
    • Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA
    • doi: 10.1083/jcb.115.3.597
    • Frank J, Penczek P, Grassucci R, Srivastava S. 1991. Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: the distribution of ribosomal RNA. J Cell Biol 115:597-605. doi: 10.1083/jcb.115.3.597.
    • (1991) J Cell Biol , vol.115 , pp. 597-605
    • Frank, J.1    Penczek, P.2    Grassucci, R.3    Srivastava, S.4
  • 8
    • 0033377941 scopus 로고    scopus 로고
    • Review: Electron crystallography: Present excitement, a nod to the past, anticipating the future
    • doi: 10.1006/jsbi.1999.4172
    • Glaeser RM. 1999. Review: electron crystallography: present excitement, a nod to the past, anticipating the future. J Struct Biol 128:3-14. doi: 10.1006/jsbi.1999.4172.
    • (1999) J Struct Biol , vol.128 , pp. 3-14
    • Glaeser, R.M.1
  • 9
    • 51349143018 scopus 로고    scopus 로고
    • Retrospective: Radiation damage and its associated "information limitations"
    • doi: 10.1016/j.jsb.2008.06.001
    • Glaeser RM. 2008. Retrospective: radiation damage and its associated "information limitations". J Struct Biol 163:271-6. doi: 10.1016/j.jsb.2008.06.001.
    • (2008) J Struct Biol , vol.163 , pp. 271-276
    • Glaeser, R.M.1
  • 10
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • doi: 10.1016/j.sbi.2011.01.008
    • Grigorieff N, Harrison SC. 2011. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy. Curr Opin Struct Biol 21:265-73. doi: 10.1016/j.sbi.2011.01.008.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.2
  • 11
    • 0018333925 scopus 로고
    • Radiation damage of purple membrane at low temperature
    • doi: 10.1016/S0304-3991(79)90211-0
    • Hayward SB, Glaeser RM. 1979. Radiation damage of purple membrane at low temperature. Ultramicroscopy 04:201-10. doi: 10.1016/S0304-3991(79)90211-0.
    • (1979) Ultramicroscopy , vol.4 , pp. 201-210
    • Hayward, S.B.1    Glaeser, R.M.2
  • 12
    • 0026523919 scopus 로고
    • Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice
    • doi: 10.1016/0304-3991(92)90003-3
    • Henderson R. 1992. Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicroscopy 46:1-18. doi: 10.1016/0304-3991(92)90003-3.
    • (1992) Ultramicroscopy , vol.46 , pp. 1-18
    • Henderson, R.1
  • 13
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • doi: 10.1017/S003358350000305X
    • Henderson R. 1995. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q Rev Biophys 28:171-93. doi: 10.1017/S003358350000305X.
    • (1995) Q Rev Biophys , vol.28 , pp. 171-193
    • Henderson, R.1
  • 14
    • 80855132610 scopus 로고    scopus 로고
    • Tilt-pair analysis of images from a range of different specimens in single-particle electron cryomicroscopy
    • doi: 10.1016/j.jmb.2011.09.008
    • Henderson R, Chen S, Chen JZ, Grigorieff N, Passmore LA, Ciccarelli L, et al. 2011. Tilt-pair analysis of images from a range of different specimens in single-particle electron cryomicroscopy. J Mol Biol 413:1028-46. doi: 10.1016/j.jmb.2011.09.008.
    • (2011) J Mol Biol , vol.413 , pp. 1028-1046
    • Henderson, R.1    Chen, S.2    Chen, J.Z.3    Grigorieff, N.4    Passmore, L.A.5    Ciccarelli, L.6
  • 15
    • 0029123968 scopus 로고
    • Cryo-electron energy loss spectroscopy: Observations on vitrified hydrated specimens and radiation damage
    • doi: 10.1016/0304-3991(95)00019-W
    • Leapman RD, Sun S. 1995. Cryo-electron energy loss spectroscopy: observations on vitrified hydrated specimens and radiation damage. Ultramicroscopy 59:71-9. doi: 10.1016/0304-3991(95)00019-W.
    • (1995) Ultramicroscopy , vol.59 , pp. 71-79
    • Leapman, R.D.1    Sun, S.2
  • 16
    • 67650544797 scopus 로고    scopus 로고
    • Detective quantum efficiency of electron area detectors in electron microscopy
    • doi: 10.1016/j.ultramic.2009.04.002
    • McMullan G, Chen S, Henderson R, Faruqi AR. 2009a. Detective quantum efficiency of electron area detectors in electron microscopy. Ultramicroscopy 109:1126-43. doi: 10.1016/j.ultramic.2009.04.002.
    • (2009) Ultramicroscopy , vol.109 , pp. 1126-1143
    • McMullan, G.1    Chen, S.2    Henderson, R.3    Faruqi, A.R.4
  • 17
    • 70349970912 scopus 로고    scopus 로고
    • Enhanced imaging in low dose electron microscopy using electron counting
    • doi: 10.1016/j.ultramic.2009.07.004
    • McMullan G, Clark AT, Turchetta R, Faruqi AR. 2009b. Enhanced imaging in low dose electron microscopy using electron counting. Ultramicroscopy 109:1411-6. doi: 10.1016/j.ultramic.2009.07.004.
    • (2009) Ultramicroscopy , vol.109 , pp. 1411-1416
    • McMullan, G.1    Clark, A.T.2    Turchetta, R.3    Faruqi, A.R.4
  • 18
    • 67650538546 scopus 로고    scopus 로고
    • Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector
    • doi: 10.1016/j.ultramic.2009.05.005
    • McMullan G, Faruqi AR, Henderson R, Guerrini N, Turchetta R, Jacobs A, et al. 2009c. Experimental observation of the improvement in MTF from backthinning a CMOS direct electron detector. Ultramicroscopy 109:1144-7. doi: 10.1016/j.ultramic.2009.05.005.
    • (2009) Ultramicroscopy , vol.109 , pp. 1144-1147
    • McMullan, G.1    Faruqi, A.R.2    Henderson, R.3    Guerrini, N.4    Turchetta, R.5    Jacobs, A.6
  • 19
    • 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 JA, Grigorieff N. 2003. Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-47. doi: 10.1016/S1047-8477(03)00069-8.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 20
    • 80052041441 scopus 로고    scopus 로고
    • Another 60 years in electron microscopy: Development of phase-plate electron microscopy and biological applications
    • doi: 10.1093/jmicro/dfr037
    • Nagayama K. 2011. Another 60 years in electron microscopy: development of phase-plate electron microscopy and biological applications. J Electron Microsc 60:S43-62. doi: 10.1093/jmicro/dfr037.
    • (2011) J Electron Microsc , vol.60
    • Nagayama, K.1
  • 21
  • 22
    • 19244372792 scopus 로고    scopus 로고
    • A 512×512 CMOS monolithic active pixel sensor with integrated ADCs for space science
    • doi: 10.1016/S0168-9002(03)01914-4
    • Prydderch M, Waltham N, Turchetta R, French M, Holt R, Marshall A, et al. 2003. A 512×512 CMOS monolithic active pixel sensor with integrated ADCs for space science. Nucl Instrum Methods Phys Res A 512:358-67. doi: 10.1016/S0168-9002(03)01914-4.
    • (2003) Nucl Instrum Methods Phys Res A , vol.512 , pp. 358-367
    • Prydderch, M.1    Waltham, N.2    Turchetta, R.3    French, M.4    Holt, R.5    Marshall, A.6
  • 23
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R. 2003. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-45.
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 24
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • doi: 10.1016/j.jmb.2011.11.010
    • Scheres SHW. 2012a. A Bayesian view on cryo-EM structure determination. J Mol Biol 415:406-18. doi: 10.1016/j.jmb.2011.11.010.
    • (2012) J Mol Biol , vol.415 , pp. 406-418
    • Scheres, S.H.W.1
  • 25
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • doi: 10.1016/j.jsb.2012.09.006
    • Scheres SHW. 2012b. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-30. doi: 10.1016/j.jsb.2012.09.006.
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 26
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • doi: 10.1038/nmeth.2115
    • Scheres SHW, Chen S. 2012. Prevention of overfitting in cryo-EM structure determination. Nat Methods 9:853-4. doi: 10.1038/nmeth.2115.
    • (2012) Nat Methods , vol.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 27
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • doi: 10.1038/nmeth992
    • Scheres SHW, Gao H, Valle M, Herman GT, Eggermont PPB, Frank J, et al. 2007. Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat Methods 4:27-9. doi: 10.1038/nmeth992.
    • (2007) Nat Methods , vol.4 , pp. 27-29
    • Scheres, S.H.W.1    Gao, H.2    Valle, M.3    Herman, G.T.4    Eggermont, P.P.B.5    Frank, J.6
  • 28
    • 71549124362 scopus 로고    scopus 로고
    • Structural insight into nascent polypeptide chain-mediated translational stalling
    • doi: 10.1126/science.1177662
    • Seidelt B, Innis CA, Wilson DN, Gartmann M, Armache J-P, Villa E, et al. 2009. Structural insight into nascent polypeptide chain-mediated translational stalling. Science 326:1412-5. doi: 10.1126/science.1177662.
    • (2009) Science , vol.326 , pp. 1412-1415
    • Seidelt, B.1    Innis, C.A.2    Wilson, D.N.3    Gartmann, M.4    Armache, J.-P.5    Villa, E.6
  • 29
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • doi: 10.1126/science.1131127
    • Selmer M, Dunham CM, Murphy FV IV, Weixlbaumer A, Petry S, Kelley AC, et al. 2006. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313:1935-42. doi: 10.1126/science.1131127.
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1    Dunham, C.M.2    Murphy IV, F.V.3    Weixlbaumer, A.4    Petry, S.5    Kelley, A.C.6
  • 30
    • 33748775731 scopus 로고    scopus 로고
    • Automated cryoEM data acquisition and analysis of 284742 particles of GroEL
    • doi: 10.1016/j.jsb.2006.04.005
    • Stagg SM, Lander GC, Pulokas J, Fellmann D, Cheng A, Quispe JD, et al. 2006. Automated cryoEM data acquisition and analysis of 284742 particles of GroEL. J Struct Biol 155:470-81. doi: 10.1016/j.jsb.2006.04.005.
    • (2006) J Struct Biol , vol.155 , pp. 470-481
    • Stagg, S.M.1    Lander, G.C.2    Pulokas, J.3    Fellmann, D.4    Cheng, A.5    Quispe, J.D.6
  • 31
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • doi: 10.1016/j.jsb.2006.05.009
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, et al. 2007. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. doi: 10.1016/j.jsb.2006.05.009.G
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6
  • 32
    • 55849143658 scopus 로고    scopus 로고
    • Insights into translational termination from the structure of RF2 bound to the ribosome
    • doi: 10.1126/science.1164840
    • Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, et al. 2008. Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322:953-56. doi: 10.1126/science.1164840.
    • (2008) Science , vol.322 , pp. 953-956
    • Weixlbaumer, A.1    Jin, H.2    Neubauer, C.3    Voorhees, R.M.4    Petry, S.5    Kelley, A.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.