메뉴 건너뛰기




Volumn 186, Issue 1, 2014, Pages 122-131

Web server for tilt-pair validation of single particle maps from electron cryomicroscopy

Author keywords

Electron cryomicroscopy; Map validation; Model bias; Tilt pair

Indexed keywords

ARTICLE; CALCULATION; COMPUTER PROGRAM; CRYOELECTRON MICROSCOPY; IMAGE QUALITY; MICROSCOPE; MICROSCOPE IMAGE; PRIORITY JOURNAL; VALIDATION STUDY; ALGORITHM; CHEMICAL STRUCTURE; INTERNET; PROCEDURES; PROTEIN QUATERNARY STRUCTURE; THREE DIMENSIONAL IMAGING; ULTRASTRUCTURE;

EID: 84898601534     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2014.02.012     Document Type: Article
Times cited : (17)

References (31)
  • 1
    • 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. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife 2013, 2:e00461.
    • (2013) eLife , vol.2
    • Bai, X.C.1    Fernandez, I.S.2    McMullan, G.3    Scheres, S.H.4
  • 2
    • 76749094569 scopus 로고    scopus 로고
    • The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals
    • Baker L.A., Smith E.A., Bueler S.A., Rubinstein J.L. The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals. J. Struct. Biol. 2010, 169:431-437.
    • (2010) J. Struct. Biol. , vol.169 , pp. 431-437
    • Baker, L.A.1    Smith, E.A.2    Bueler, S.A.3    Rubinstein, J.L.4
  • 4
    • 0021206682 scopus 로고
    • Methods for specimen thickness determination in electron microscopy
    • Berriman J., Bryan R.K., Freeman R., Leonard K.R. Methods for specimen thickness determination in electron microscopy. Ultramicroscopy 1984, 13:351-364.
    • (1984) Ultramicroscopy , vol.13 , pp. 351-364
    • Berriman, J.1    Bryan, R.K.2    Freeman, R.3    Leonard, K.R.4
  • 6
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen S., McMullan G., Faruqi A.R., Murshudov G.N., Short J.M., Scheres S.H., Henderson R. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 2013, 135:24-35.
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1    McMullan, G.2    Faruqi, A.R.3    Murshudov, G.N.4    Short, J.M.5    Scheres, S.H.6    Henderson, R.7
  • 7
    • 0345599153 scopus 로고    scopus 로고
    • Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus
    • Crowther R.A., Berriman J.A., Curran W.L., Allan G.M., Todd D. Comparison of the structures of three circoviruses: chicken anemia virus, porcine circovirus type 2, and beak and feather disease virus. J. Virol. 2003, 77:13036-13041.
    • (2003) J. Virol. , vol.77 , pp. 13036-13041
    • Crowther, R.A.1    Berriman, J.A.2    Curran, W.L.3    Allan, G.M.4    Todd, D.5
  • 9
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D 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 3D electron microscopy and related fields. J. Struct. Biol. 1996, 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 10
    • 0032540273 scopus 로고    scopus 로고
    • Three-dimensional structure of bovine NADH: ubiquinone oxidoreductase (complex I) at 22 Å in ice
    • Grigorieff N. Three-dimensional structure of bovine NADH: ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 1998, 277:1033-1046.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1033-1046
    • Grigorieff, N.1
  • 11
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN: high-resolution refinement of single particle structures
    • Grigorieff N. FREALIGN: high-resolution refinement of single particle structures. J. Struct. Biol. 2007, 157:117-125.
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 12
    • 79953108462 scopus 로고    scopus 로고
    • Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy
    • Grigorieff N., Harrison S.C. Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy. Curr. Opin. Struct. Biol. 2011, 21:265-273.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 265-273
    • Grigorieff, N.1    Harrison, S.C.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, 28:171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 14
    • 84876978430 scopus 로고    scopus 로고
    • Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice
    • Henderson R., McMullan G. Problems in obtaining perfect images by single-particle electron cryomicroscopy of biological structures in amorphous ice. J. Electron Microsc. 2013, 62:43-50.
    • (2013) J. Electron Microsc. , vol.62 , pp. 43-50
    • Henderson, R.1    McMullan, G.2
  • 17
    • 23044475632 scopus 로고    scopus 로고
    • Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology
    • Heymann J.B., Chagoyen M., Belnap D.M. Common conventions for interchange and archiving of three-dimensional electron microscopy information in structural biology. J. Struct. Biol. 2005, 151:196-207.
    • (2005) J. Struct. Biol. , vol.151 , pp. 196-207
    • Heymann, J.B.1    Chagoyen, M.2    Belnap, D.M.3
  • 18
  • 21
    • 83755207591 scopus 로고    scopus 로고
    • Structural analysis of macromolecular assemblies by electron microscopy
    • Orlova E.V., Saibil H.R. Structural analysis of macromolecular assemblies by electron microscopy. Chem. Rev. 2011, 111:7710-7748.
    • (2011) Chem. Rev. , vol.111 , pp. 7710-7748
    • Orlova, E.V.1    Saibil, H.R.2
  • 23
    • 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
  • 24
    • 77957322190 scopus 로고    scopus 로고
    • Classification of structural heterogeneity by maximum-likelihood methods
    • Scheres S.H. Classification of structural heterogeneity by maximum-likelihood methods. Methods Enzymol. 2010, 482:295-320.
    • (2010) Methods Enzymol. , vol.482 , pp. 295-320
    • Scheres, S.H.1
  • 25
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres S.H., Chen S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 2012, 9:853-854.
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 26
    • 0037404096 scopus 로고    scopus 로고
    • An approach to examining model dependence in EM reconstructions using cross-validation
    • Shaikh T.R., Hegerl R., Frank J. An approach to examining model dependence in EM reconstructions using cross-validation. J. Struct. Biol. 2003, 142:301-310.
    • (2003) J. Struct. Biol. , vol.142 , pp. 301-310
    • Shaikh, T.R.1    Hegerl, R.2    Frank, J.3
  • 27
    • 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, 122:328-339.
    • (1998) J. Struct. Biol. , vol.122 , pp. 328-339
    • Sigworth, F.J.1
  • 29
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • Stewart A., Grigorieff N. Noise bias in the refinement of structures derived from single particles. Ultramicroscopy 2004, 102:67-84.
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 30
    • 84867010573 scopus 로고    scopus 로고
    • Automatic magnification determination of electron cryomicroscopy images using apoferritin as a standard
    • Wasilewski S., Karelina D., Berriman J.A., Rosenthal P.B. Automatic magnification determination of electron cryomicroscopy images using apoferritin as a standard. J. Struct. Biol. 2012, 180:243-248.
    • (2012) J. Struct. Biol. , vol.180 , pp. 243-248
    • Wasilewski, S.1    Karelina, D.2    Berriman, J.A.3    Rosenthal, P.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.