메뉴 건너뛰기




Volumn 157, Issue 1, 2007, Pages 201-210

Ab initio resolution measurement for single particle structures

Author keywords

Electron microscopy; Protein structure; Resolution measurement; RMEASURE; Single particle

Indexed keywords

AB INITIO CALCULATION; ARTICLE; CALCULATION; COMPUTER PROGRAM; CORRELATION ANALYSIS; ELECTRON MICROSCOPY; FOURIER ANALYSIS; MATHEMATICAL COMPUTING; MEASUREMENT; PRIORITY JOURNAL; SIGNAL NOISE RATIO; STRUCTURE ANALYSIS;

EID: 33845291163     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.08.003     Document Type: Article
Times cited : (94)

References (28)
  • 1
    • 0022759777 scopus 로고
    • Effect of errors, redundancy, and solvent content in the molecular replacement procedure for the structure determination of biological macromolecules
    • Arnold E., and Rossmann M.G. Effect of errors, redundancy, and solvent content in the molecular replacement procedure for the structure determination of biological macromolecules. Proc. Natl. Acad. Sci. USA 83 (1986) 5489-5493
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5489-5493
    • Arnold, E.1    Rossmann, M.G.2
  • 2
    • 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., and Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386 (1997) 88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 3
    • 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., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 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
  • 4
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • Frank J., Verschoor A., and Boublik M. Computer averaging of electron micrographs of 40S ribosomal subunits. Science 214 (1981) 1353-1355
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 6
    • 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. 56 Pt 10 (2000) 1270-1277
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PART 10 , pp. 1270-1277
    • Grigorieff, N.1
  • 7
    • 33845304442 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. (2006)
    • (2006) J. Struct. Biol.
    • Grigorieff, N.1
  • 9
    • 0000313739 scopus 로고
    • Exact filters for general geometry 3-dimensional reconstruction
    • Harauz G., and van Heel M. Exact filters for general geometry 3-dimensional reconstruction. Optik 73 (1986) 146-156
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 10
    • 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 (1995) 171-193
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 11
    • 1442360371 scopus 로고    scopus 로고
    • Three-dimensional structure of C complex spliceosomes by electron microscopy
    • Jurica M.S., Sousa D., Moore M.J., and Grigorieff N. Three-dimensional structure of C complex spliceosomes by electron microscopy. Nat. Struct. Mol. Biol. 11 (2004) 265-269
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 265-269
    • Jurica, M.S.1    Sousa, D.2    Moore, M.J.3    Grigorieff, N.4
  • 12
    • 0035423087 scopus 로고    scopus 로고
    • The kink-turn: a new RNA secondary structure motif
    • Klein D.J., Schmeing T.M., Moore P.B., and Steitz T.A. The kink-turn: a new RNA secondary structure motif. EMBO J. 20 (2001) 4214-4221
    • (2001) EMBO J. , vol.20 , pp. 4214-4221
    • Klein, D.J.1    Schmeing, T.M.2    Moore, P.B.3    Steitz, T.A.4
  • 13
    • 27944481316 scopus 로고    scopus 로고
    • Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35
    • Laurinmaki P.A., Huiskonen J.T., Bamford D.H., and Butcher S.J. Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35. Structure 13 (2005) 1819-1828
    • (2005) Structure , vol.13 , pp. 1819-1828
    • Laurinmaki, P.A.1    Huiskonen, J.T.2    Bamford, D.H.3    Butcher, S.J.4
  • 14
    • 3142538754 scopus 로고    scopus 로고
    • Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy
    • Ludtke S.J., Chen D.H., Song J.L., Chuang D.T., and Chiu W. Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy. Structure 12 (2004) 1129-1136
    • (2004) Structure , vol.12 , pp. 1129-1136
    • Ludtke, S.J.1    Chen, D.H.2    Song, J.L.3    Chuang, D.T.4    Chiu, W.5
  • 15
    • 0035825140 scopus 로고    scopus 로고
    • Molecular machines: putting the pieces together
    • Nogales E., and Grigorieff N. Molecular machines: putting the pieces together. J. Cell Biol. 152 (2001) F1-F10
    • (2001) J. Cell Biol. , vol.152
    • Nogales, E.1    Grigorieff, N.2
  • 16
    • 0028393194 scopus 로고
    • The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    • Penczek P.A., Grassucci R.A., and Frank J. The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles. Ultramicroscopy 53 (1994) 251-270
    • (1994) Ultramicroscopy , vol.53 , pp. 251-270
    • Penczek, P.A.1    Grassucci, R.A.2    Frank, J.3
  • 17
    • 33644847296 scopus 로고    scopus 로고
    • Estimation of variance in single-particle reconstruction using the bootstrap technique
    • Penczek P.A., Yang C., Frank J., and Spahn C.M. Estimation of variance in single-particle reconstruction using the bootstrap technique. J. Struct. Biol. 154 (2006) 168-183
    • (2006) J. Struct. Biol. , vol.154 , pp. 168-183
    • Penczek, P.A.1    Yang, C.2    Frank, J.3    Spahn, C.M.4
  • 18
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., and Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333 (2003) 721-745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 19
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M., Wagenknecht T., and Allen P.D. Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat. Struct. Mol. Biol. 12 (2005) 539-544
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 20
    • 0037404096 scopus 로고    scopus 로고
    • An approach to examining model dependence in EM reconstructions using cross-validation
    • Shaikh T.R., Hegerl R., and Frank J. An approach to examining model dependence in EM reconstructions using cross-validation. J. Struct. Biol. 142 (2003) 301-310
    • (2003) J. Struct. Biol. , vol.142 , pp. 301-310
    • Shaikh, T.R.1    Hegerl, R.2    Frank, J.3
  • 21
    • 0035078574 scopus 로고    scopus 로고
    • Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution
    • Sokolova O., Kolmakova-Partensky L., and Grigorieff N. Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution. Structure (Camb) 9 (2001) 215-220
    • (2001) Structure (Camb) , vol.9 , pp. 215-220
    • Sokolova, O.1    Kolmakova-Partensky, L.2    Grigorieff, N.3
  • 22
    • 0034665245 scopus 로고    scopus 로고
    • A method for differentiating proteins from nucleic acids in intermediate-resolution density maps: cryo-electron microscopy defines the quaternary structure of the Escherichia coli 70S ribosome
    • Spahn C.M., Penczek P.A., Leith A., and Frank J. A method for differentiating proteins from nucleic acids in intermediate-resolution density maps: cryo-electron microscopy defines the quaternary structure of the Escherichia coli 70S ribosome. Structure 8 (2000) 937-948
    • (2000) Structure , vol.8 , pp. 937-948
    • Spahn, C.M.1    Penczek, P.A.2    Leith, A.3    Frank, J.4
  • 23
    • 8844219659 scopus 로고    scopus 로고
    • Noise bias in the refinement of structures derived from single particles
    • Stewart A., and Grigorieff N. Noise bias in the refinement of structures derived from single particles. Ultramicroscopy 102 (2004) 67-84
    • (2004) Ultramicroscopy , vol.102 , pp. 67-84
    • Stewart, A.1    Grigorieff, N.2
  • 24
    • 0024698772 scopus 로고
    • The spectral signal-to-noise ratio resolution criterion: computational efficiency and statistical precision
    • Unser M., Trus B.L., Frank J., and Steven A.C. The spectral signal-to-noise ratio resolution criterion: computational efficiency and statistical precision. Ultramicroscopy 30 (1989) 429-433
    • (1989) Ultramicroscopy , vol.30 , pp. 429-433
    • Unser, M.1    Trus, B.L.2    Frank, J.3    Steven, A.C.4
  • 25
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signal-to-noise ratios
    • Unser M., Trus B.L., and Steven A.C. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicroscopy 23 (1987) 39-51
    • (1987) Ultramicroscopy , vol.23 , pp. 39-51
    • Unser, M.1    Trus, B.L.2    Steven, A.C.3
  • 26
    • 0026566945 scopus 로고
    • A brief look at imaging and contrast transfer
    • Wade R.H. A brief look at imaging and contrast transfer. Ultramicroscopy 46 (1992) 145-156
    • (1992) Ultramicroscopy , vol.46 , pp. 145-156
    • Wade, R.H.1
  • 27
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A
    • Zhang X., Walker S.B., Chipman P.R., Nibert M.L., and Baker T.S. Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A. Nat. Struct. Biol. 10 (2003) 1011-1018
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.