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Volumn 12, Issue 2, 2017, Pages 209-212

Advances in the field of single-particle cryo-electron microscopy over the last decade

Author keywords

[No Author keywords available]

Indexed keywords

AUTOMATION; CRYOELECTRON MICROSCOPY; ELECTRON MICROSCOPE; ESCHERICHIA COLI; IMAGE RECONSTRUCTION; MEDICAL LITERATURE; METHODOLOGY; NONHUMAN; PUBLICATION; REVIEW; RIBOSOME; SINGLE PARTICLE CRYOELECTRON MICROSCOPY; SOFTWARE; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; TRYPANOSOMA CRUZI; X RAY CRYSTALLOGRAPHY; DEVICES; PROCEDURES; SIGNAL NOISE RATIO;

EID: 85010949829     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2017.004     Document Type: Review
Times cited : (121)

References (30)
  • 1
    • 39149091041 scopus 로고    scopus 로고
    • Preparation of macromolecular complexes for cryo-electron microscopy
    • Grassucci, R.A., Taylor, D.J. & Frank, J. Preparation of macromolecular complexes for cryo-electron microscopy. Nat. Protoc. 2, 3239-3246 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 3239-3246
    • Grassucci, R.A.1    Taylor, D.J.2    Frank, J.3
  • 2
    • 39449126462 scopus 로고    scopus 로고
    • Visualization of macromolecular complexes using cryo-electron microscopy with FEI Tecnai transmission electron microscopes
    • Grassucci, R.A., Taylor, D. & Frank, J. Visualization of macromolecular complexes using cryo-electron microscopy with FEI Tecnai transmission electron microscopes. Nat. Protoc. 3, 330-339 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 330-339
    • Grassucci, R.A.1    Taylor, D.2    Frank, J.3
  • 3
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T.R. et al. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1
  • 4
    • 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 16, 673-683 (2008).
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 5
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • Scheres, S.H.W. et al. Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat. Methods 4, 27-29 (2007).
    • (2007) Nat. Methods , vol.4 , pp. 27-29
    • Scheres, S.H.W.1
  • 6
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • Scheres, S.H.W. A Bayesian view on cryo-EM structure determination. J. Mol. Biol. 415, 406-418 (2012).
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.W.1
  • 7
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang, X., Jin, L., Fang, Q., Hui, W.H. & Zhou, Z.H. 3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141, 472-482 (2010).
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 8
    • 51549117861 scopus 로고    scopus 로고
    • Exploration of parameters in cryo-EM leading to an improved density map of the E. Coli ribosome
    • LeBarron, J. et al. Exploration of parameters in cryo-EM leading to an improved density map of the E. coli ribosome. J. Struct. Biol. 164, 24-32 (2008).
    • (2008) J. Struct. Biol. , vol.164 , pp. 24-32
    • LeBarron, J.1
  • 9
    • 59049096394 scopus 로고    scopus 로고
    • Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis
    • Villa, E. et al. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc. Natl. Acad. Sci. USA 106, 1063-1068 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1063-1068
    • Villa, E.1
  • 10
    • 84874191297 scopus 로고    scopus 로고
    • High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome
    • Hashem, Y. et al. High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome. Nature 494, 385-389 (2013).
    • (2013) Nature , vol.494 , pp. 385-389
    • Hashem, Y.1
  • 11
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R. The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28, 171-193 (1995).
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 12
    • 0029100747 scopus 로고
    • A model of protein synthesis based on cryo-electron microscopy of the E. Coli ribosome
    • Frank, J. et al. A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376, 441-444 (1995).
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1
  • 13
    • 84878580683 scopus 로고    scopus 로고
    • Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
    • Bai, X.C., Fernandez, I.S., McMullan, G. & Scheres, S.H.W. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife 2, e00461 (2013).
    • (2013) ELife , vol.2 , pp. e00461
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.W.4
  • 14
    • 84992345994 scopus 로고    scopus 로고
    • Structure and assembly model for the Trypanosoma cruzi 60S ribosomal subunit
    • Liu, Z. et al. Structure and assembly model for the Trypanosoma cruzi 60S ribosomal subunit. Proc. Natl. Acad. Sci. USA 113, 12174-12179 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. 12174-12179
    • Liu, Z.1
  • 15
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 16
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118 (2013).
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 17
    • 84862255790 scopus 로고    scopus 로고
    • Spotiton: A prototype for an integrated inkjet dispense and vitrification system for cryo-TEM
    • Jain, T., Sheehan, P., Crum, J., Carragher, B. & Potter, C.S. Spotiton: a prototype for an integrated inkjet dispense and vitrification system for cryo-TEM. J. Struct. Biol. 179, 68-75 (2012).
    • (2012) J. Struct. Biol. , vol.179 , pp. 68-75
    • Jain, T.1    Sheehan, P.2    Crum, J.3    Carragher, B.4    Potter, C.S.5
  • 18
    • 84992046823 scopus 로고    scopus 로고
    • A new method for vitrifying samples for cryoEM
    • Razinkov, I. et al. A new method for vitrifying samples for cryoEM. J. Struct. Biol. 195, 190-198 (2016).
    • (2016) J. Struct. Biol. , vol.195 , pp. 190-198
    • Razinkov, I.1
  • 19
    • 84917709175 scopus 로고    scopus 로고
    • Electron microscopy: Ultrastable gold substrates for electron cryomicroscopy
    • Russo, C.J. & Passmore, L.A. Electron microscopy: ultrastable gold substrates for electron cryomicroscopy. Science 346, 1377-1380 (2014).
    • (2014) Science , vol.346 , pp. 1377-1380
    • Russo, C.J.1    Passmore, L.A.2
  • 20
    • 84954217129 scopus 로고    scopus 로고
    • Progress towards an optimal specimen support for electron cryomicroscopy
    • Russo, C.J. & Passmore, L.A. Progress towards an optimal specimen support for electron cryomicroscopy. Curr. Opin. Struct. Biol. 37, 81-89 (2016).
    • (2016) Curr. Opin. Struct. Biol. , vol.37 , pp. 81-89
    • Russo, C.J.1    Passmore, L.A.2
  • 22
    • 84968725663 scopus 로고    scopus 로고
    • Cryo-EM single particle analysis with the Volta phase plate
    • Danev, R. & Baumeister, W. Cryo-EM single particle analysis with the Volta phase plate. eLife 5, e13046 (2016).
    • (2016) ELife , vol.5 , pp. e13046
    • Danev, R.1    Baumeister, W.2
  • 23
    • 70350234771 scopus 로고    scopus 로고
    • Monolithic microfluidic mixing-spraying devices for time-resolved cryo-electron microscopy
    • Lu, Z. et al. Monolithic microfluidic mixing-spraying devices for time-resolved cryo-electron microscopy. J. Struct. Biol. 168, 388-395 (2009).
    • (2009) J. Struct. Biol. , vol.168 , pp. 388-395
    • Lu, Z.1
  • 24
    • 84930273910 scopus 로고    scopus 로고
    • Structural dynamics of ribosome subunit association studied by mixing-spraying time-resolved cryogenic electron microscopy
    • Chen, B. et al. Structural dynamics of ribosome subunit association studied by mixing-spraying time-resolved cryogenic electron microscopy. Structure 23, 1097-1105 (2015).
    • (2015) Structure , vol.23 , pp. 1097-1105
    • Chen, B.1
  • 25
    • 85002291937 scopus 로고    scopus 로고
    • Key intermediates in ribosome recycling visualized by timeresolved cryoelectron microscopy
    • Fu, Z. et al. Key intermediates in ribosome recycling visualized by timeresolved cryoelectron microscopy. Structure 24, 2092-2101 (2016).
    • (2016) Structure , vol.24 , pp. 2092-2101
    • Fu, Z.1
  • 26
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human g-secretase
    • Bai, X., Rajendra, E., Yang, G., Shi, Y. & Scheres, S.H.W. Sampling the conformational space of the catalytic subunit of human g-secretase. eLife 4, e11182 (2015)
    • (2015) ELife , vol.4 , pp. e11182
    • Bai, X.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.W.5
  • 27
    • 85002397042 scopus 로고    scopus 로고
    • Determination of the ribosome structure to a resolution of 2.5 A by single-particle cryo-EM
    • Liu, Z. et al. Determination of the ribosome structure to a resolution of 2.5 A by single-particle cryo-EM. Protein Sci. http://dx.doi.org/10.1002/pro.306 (2016).
    • (2016) Protein Sci.
    • Liu, Z.1
  • 28
    • 33845361023 scopus 로고    scopus 로고
    • Structure of the ribosome-bound cricket paralysis virus IRES RNA
    • Schüler, M. et al. Structure of the ribosome-bound cricket paralysis virus IRES RNA. Nat. Struct. Mol. Biol. 13, 1092-1096 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1092-1096
    • Schüler, M.1
  • 29
    • 78650546283 scopus 로고    scopus 로고
    • Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution
    • Armache, J.P. et al. Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution. Proc. Natl. Acad. Sci. USA 107, 19748-19753 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 19748-19753
    • Armache, J.P.1
  • 30
    • 84905080837 scopus 로고    scopus 로고
    • Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine
    • Wong, W. et al. Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. eLife 3, e03080 (2014).
    • (2014) ELife , vol.3 , pp. e03080
    • Wong, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.