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Volumn 190, Issue 2, 2015, Pages 215-223

Conical fourier shell correlation applied to electron tomograms

Author keywords

Conical fourier shell correlation; Cryo electron microscopy; Dual axis cryo electron tomography; Fourier shell correlation; Resolution estimation

Indexed keywords

ARTICLE; CONTROLLED STUDY; ELECTRON BEAM; ELECTRON RADIATION; ELECTRON TOMOGRAPHY; IMAGE RECONSTRUCTION; NONHUMAN; PRIORITY JOURNAL; SIMULATION; ANISOTROPY; COMPARATIVE STUDY; COMPUTER SIMULATION; CRYOELECTRON MICROSCOPY; FOURIER ANALYSIS; IMAGE PROCESSING; PROCEDURES; RADIATION RESPONSE;

EID: 84928694869     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2015.03.010     Document Type: Article
Times cited : (21)

References (40)
  • 2
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Boettcher B., Wynne S.A., Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 1997, 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Boettcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 3
    • 0000484921 scopus 로고
    • Inversion of fan-beam scans in radio astronomy
    • Bracewell R.N., Riddle A.C. Inversion of fan-beam scans in radio astronomy. Astrophys J 1967, 150:427.
    • (1967) Astrophys J , vol.150 , pp. 427
    • Bracewell, R.N.1    Riddle, A.C.2
  • 5
    • 23044510524 scopus 로고    scopus 로고
    • A resolution criterion for electron tomography based on cross-validation
    • Cardone G., Grünewald K., Steven A.C. A resolution criterion for electron tomography based on cross-validation. J. Struct. Biol. 2005, 151:117-129.
    • (2005) J. Struct. Biol. , vol.151 , pp. 117-129
    • Cardone, G.1    Grünewald, K.2    Steven, A.C.3
  • 6
    • 84892772002 scopus 로고    scopus 로고
    • On resolution in electron tomography of beam sensitive materials
    • Chen D., Friedrich H., With G.d. On resolution in electron tomography of beam sensitive materials. J. Phys. Chem. C 2014, 118:1248-1257.
    • (2014) J. Phys. Chem. C , vol.118 , pp. 1248-1257
    • Chen, D.1    Friedrich, H.2    With, G.3
  • 8
    • 84866145467 scopus 로고    scopus 로고
    • Pushing the resolution limits in cryo electron tomography of biological structures
    • Diebolder C.A., Koster A.J., Koning R.I. Pushing the resolution limits in cryo electron tomography of biological structures. J. Microsc. 2012, 248:1-5.
    • (2012) J. Microsc. , vol.248 , pp. 1-5
    • Diebolder, C.A.1    Koster, A.J.2    Koning, R.I.3
  • 11
    • 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, 106:587-596.
    • (2006) Ultramicroscopy , vol.106 , pp. 587-596
    • Fernandez, J.J.1    Li, S.2    Crowther, R.A.3
  • 12
    • 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, 135:239-250.
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 13
    • 0016789772 scopus 로고
    • Signal-to-noise ratio of electron micrographs obtained by cross correlation
    • Frank J., Al-Ali L. Signal-to-noise ratio of electron micrographs obtained by cross correlation. Nature 1975, 256:376-379.
    • (1975) Nature , vol.256 , pp. 376-379
    • Frank, J.1    Al-Ali, L.2
  • 14
    • 84873198809 scopus 로고    scopus 로고
    • Single versus dual-axis cryo-electron tomography of microtubules assembled in vitro: limits and perspectives
    • Guesdon A., Blestel S., Kervrann C., Crétien D. Single versus dual-axis cryo-electron tomography of microtubules assembled in vitro: limits and perspectives. J. Struct. Biol. 2013, 181:169-178.
    • (2013) J. Struct. Biol. , vol.181 , pp. 169-178
    • Guesdon, A.1    Blestel, S.2    Kervrann, C.3    Crétien, D.4
  • 16
    • 79551635109 scopus 로고    scopus 로고
    • A practical method to determine the effective resolution in incoherent experimental electron tomography
    • Heidari Mezerji H., Van den Broek W., Bals S. A practical method to determine the effective resolution in incoherent experimental electron tomography. Ultramicroscopy 2011, 111:330-336.
    • (2011) Ultramicroscopy , vol.111 , pp. 330-336
    • Heidari Mezerji, H.1    Van den Broek, W.2    Bals, S.3
  • 17
    • 0010196138 scopus 로고    scopus 로고
    • DIPimage: A Scientific Image Processing Toolbox for MATLAB. Quantitative Imaging Group
    • Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands.
    • Hendriks, C.L., Van Vliet, L.J., Rieger, B., van Kempen, G.M.P., van Ginkel, M. 1999. DIPimage: A Scientific Image Processing Toolbox for MATLAB. Quantitative Imaging Group, Faculty of Applied Sciences, Delft University of Technology, Delft, The Netherlands.
    • (1999)
    • Hendriks, C.L.1    Van Vliet, L.J.2    Rieger, B.3    van Kempen, G.M.P.4    van Ginkel, M.5
  • 18
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: image processing and molecular modeling for electron microscopy
    • Heymann J.B., Belnap D.M. Bsoft: image processing and molecular modeling for electron microscopy. J. Struct. Biol. 2007, 157:3-18.
    • (2007) J. Struct. Biol. , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 20
    • 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, 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 21
    • 11144223254 scopus 로고    scopus 로고
    • Conical tomography of freeze-fracture replicas: a method for the study of integral membrane proteins inserted in phospholipid bilayers
    • Lanzavecchia S., Cantele F., Bellon P.L., Zampighi L., Kreman M., Wright E., Zampighi G.A. Conical tomography of freeze-fracture replicas: a method for the study of integral membrane proteins inserted in phospholipid bilayers. J. Struct. Biol. 2005, 149:87-98.
    • (2005) J. Struct. Biol. , vol.149 , pp. 87-98
    • Lanzavecchia, S.1    Cantele, F.2    Bellon, P.L.3    Zampighi, L.4    Kreman, M.5    Wright, E.6    Zampighi, G.A.7
  • 23
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: an approach with alignment methods that preserve resolution
    • Mastronarde D.N. Dual-axis tomography: an approach with alignment methods that preserve resolution. J. Struct. Biol. 1997, 120:343-352.
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 24
    • 84873142598 scopus 로고    scopus 로고
    • Single particle and molecular assembly analysis of polyribosomes by single-and double-tilt cryo electron tomography
    • Myasnikov A.G., Afonina Z.A., Klaholz B.P. Single particle and molecular assembly analysis of polyribosomes by single-and double-tilt cryo electron tomography. Ultramicroscopy 2013, 126:33-39.
    • (2013) Ultramicroscopy , vol.126 , pp. 33-39
    • Myasnikov, A.G.1    Afonina, Z.A.2    Klaholz, B.P.3
  • 25
    • 0037288048 scopus 로고    scopus 로고
    • 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, 141:34-42.
    • (2003) J. Struct. Biol. , vol.141 , pp. 34-42
    • Nickell, S.1    Hegerl, R.2    Baumeister, W.3    Rachel, R.4
  • 26
    • 84920050380 scopus 로고    scopus 로고
    • Resolution in electron tomography
    • Penczek P.A., Frank J. Resolution in electron tomography. Electron Tomogr. 2006, 307-330.
    • (2006) Electron Tomogr. , pp. 307-330
    • Penczek, P.A.1    Frank, J.2
  • 28
    • 0036417211 scopus 로고    scopus 로고
    • Three-dimensional spectral signal-to-noise ratio for a class of reconstruction algorithms
    • Penczek P.A. Three-dimensional spectral signal-to-noise ratio for a class of reconstruction algorithms. J. Struct. Biol. 2002, 138:34-46.
    • (2002) J. Struct. Biol. , vol.138 , pp. 34-46
    • Penczek, P.A.1
  • 29
    • 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
  • 30
    • 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, 333:721-745.
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 31
    • 0031542184 scopus 로고    scopus 로고
    • Distributing many points on a sphere
    • Saff E.B., Kuijlaars A.B. Distributing many points on a sphere. Math. Intell. 1997, 19:5-11.
    • (1997) Math. Intell. , vol.19 , pp. 5-11
    • Saff, E.B.1    Kuijlaars, A.B.2
  • 32
    • 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. 1982, 127:127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 35
    • 0020014750 scopus 로고
    • Detection of objects in quantum-noise-limited images
    • van Heel M. Detection of objects in quantum-noise-limited images. Ultramicroscopy 1982, 7:331-341.
    • (1982) Ultramicroscopy , vol.7 , pp. 331-341
    • van Heel, M.1
  • 36
    • 0022734418 scopus 로고
    • Resolution criteria for three dimensional reconstruction
    • van Heel M., Harauz G. Resolution criteria for three dimensional reconstruction. Optik 1986, 73:119-122.
    • (1986) Optik , vol.73 , pp. 119-122
    • van Heel, M.1    Harauz, G.2
  • 37
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel M., Schatz M. Fourier shell correlation threshold criteria. J. Struct. Biol. 2005, 151:250-262.
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • van Heel, M.1    Schatz, M.2
  • 38
    • 84876705471 scopus 로고    scopus 로고
    • Marker-free dual-axis tilt series alignment
    • Winkler H., Taylor K.A. Marker-free dual-axis tilt series alignment. J. Struct. Biol. 2013, 182:117-124.
    • (2013) J. Struct. Biol. , vol.182 , pp. 117-124
    • Winkler, H.1    Taylor, K.A.2
  • 39
    • 70350238351 scopus 로고    scopus 로고
    • Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle
    • Wu S., Liu J., Reedy M.C., Winkler H., Reedy M.K., Taylor K.A. Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle. J. Struct. Biol. 2009, 168:485-502.
    • (2009) J. Struct. Biol. , vol.168 , pp. 485-502
    • Wu, S.1    Liu, J.2    Reedy, M.C.3    Winkler, H.4    Reedy, M.K.5    Taylor, K.A.6
  • 40
    • 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 2010, 141:472-482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.