메뉴 건너뛰기




Volumn 109, Issue 3, 2009, Pages 253-263

Reciprocal space representations of helical objects and their projection images for helices constructed from motifs without spherical symmetry

Author keywords

3 D reconstruction; Cryo electron microscopy; Helix; Motif; Symmetry

Indexed keywords

3-D RECONSTRUCTION; CRYO-ELECTRON MICROSCOPY; HELIX; MOTIF; SYMMETRY;

EID: 59649126393     PISSN: 03043991     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ultramic.2008.10.014     Document Type: Article
Times cited : (4)

References (24)
  • 1
    • 0001704671 scopus 로고
    • The structure of synthetic polypeptides. I. The transform of atoms on a helix
    • Cochran W., Crick F.H.C., and Vand V. The structure of synthetic polypeptides. I. The transform of atoms on a helix. Acta Crystallogr. 5 (1952) 581-586
    • (1952) Acta Crystallogr. , vol.5 , pp. 581-586
    • Cochran, W.1    Crick, F.H.C.2    Vand, V.3
  • 2
    • 0003056635 scopus 로고
    • Image analysis of electron micrographs
    • Hawkes P.W., and Valdrè U. (Eds), Academic Press, New York chapter 7
    • Moody M.F. Image analysis of electron micrographs. In: Hawkes P.W., and Valdrè U. (Eds). Biophysical Electron Microscopy: Basic Concepts and Modern Techniques (1990), Academic Press, New York 145-287 chapter 7
    • (1990) Biophysical Electron Microscopy: Basic Concepts and Modern Techniques , pp. 145-287
    • Moody, M.F.1
  • 3
    • 0034034591 scopus 로고    scopus 로고
    • Structure determination of tubular crystals of membrane proteins. I. Indexing of diffraction patterns
    • Toyoshima C. Structure determination of tubular crystals of membrane proteins. I. Indexing of diffraction patterns. Ultramicroscopy 84 1/2 (2000) 1-14
    • (2000) Ultramicroscopy , vol.84 , Issue.1-2 , pp. 1-14
    • Toyoshima, C.1
  • 5
    • 0345414583 scopus 로고    scopus 로고
    • A statistical approach to computer processing of cryo-electron microscope images: virion classification and 3-D reconstruction
    • Yin Z., Zheng Y., Doerschuk P.C., Natarajan P., and Johnson J.E. A statistical approach to computer processing of cryo-electron microscope images: virion classification and 3-D reconstruction. J. Struct. Biol. 144 1/2 (2003) 24-50
    • (2003) J. Struct. Biol. , vol.144 , Issue.1-2 , pp. 24-50
    • Yin, Z.1    Zheng, Y.2    Doerschuk, P.C.3    Natarajan, P.4    Johnson, J.E.5
  • 6
    • 0034245578 scopus 로고    scopus 로고
    • Ab initio reconstruction and experimental design for cryo electron microscopy
    • Doerschuk P.C., and Johnson J.E. Ab initio reconstruction and experimental design for cryo electron microscopy. IEEE Trans. Info. Theory 46 August 5 (2000) 1714-1729
    • (2000) IEEE Trans. Info. Theory , vol.46 , Issue.August 5 , pp. 1714-1729
    • Doerschuk, P.C.1    Johnson, J.E.2
  • 7
    • 34547920696 scopus 로고    scopus 로고
    • Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching
    • Parent K.N., Suhanovsky M.M., and Teschke C.M. Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching. Mol. Microbiol. 65 5 (2007) 1300-1310
    • (2007) Mol. Microbiol. , vol.65 , Issue.5 , pp. 1300-1310
    • Parent, K.N.1    Suhanovsky, M.M.2    Teschke, C.M.3
  • 8
  • 9
    • 0024974913 scopus 로고
    • Visualization of protein-nucleic acid interactions in a virus: refined structure of intact tobacco mosaic virus at 2.9 Å resolution by X-ray fiber diffraction
    • Namba K., Pattanayek R., and Stubbs G. Visualization of protein-nucleic acid interactions in a virus: refined structure of intact tobacco mosaic virus at 2.9 Å resolution by X-ray fiber diffraction. J. Mol. Biol. 208 (1989) 307-325
    • (1989) J. Mol. Biol. , vol.208 , pp. 307-325
    • Namba, K.1    Pattanayek, R.2    Stubbs, G.3
  • 10
    • 0024961660 scopus 로고
    • Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy
    • Jeng T.-W., Crowther R.A., Stubbs G., and Chiu W. Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy. J. Mol. Biol. 205 (1989) 251-257
    • (1989) J. Mol. Biol. , vol.205 , pp. 251-257
    • Jeng, T.-W.1    Crowther, R.A.2    Stubbs, G.3    Chiu, W.4
  • 11
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus
    • Sachse C., Chen J.Z., Coureux P.-D., Stroupe M.E., Fändrich M., and Grigorieff N. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J. Mol. Biol. 371 (2007) 812-835
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.Z.2    Coureux, P.-D.3    Stroupe, M.E.4    Fändrich, M.5    Grigorieff, N.6
  • 12
    • 0007459511 scopus 로고    scopus 로고
    • Iterative reconstruction of three-dimensional objects from averaged Fourier-transform magnitude: solution and fiber X-ray scattering problems
    • Zheng Y., and Doerschuk P.C. Iterative reconstruction of three-dimensional objects from averaged Fourier-transform magnitude: solution and fiber X-ray scattering problems. J. Opt. Soc. Am. A 13 7 (1996) 1483-1494
    • (1996) J. Opt. Soc. Am. A , vol.13 , Issue.7 , pp. 1483-1494
    • Zheng, Y.1    Doerschuk, P.C.2
  • 14
    • 0344270228 scopus 로고
    • The Fourier transform of an electron micrograph-first order and second order theory of image formation
    • Barer R., and Cosslett V.E. (Eds), Academic Press, London and New York
    • Erickson H.P. The Fourier transform of an electron micrograph-first order and second order theory of image formation. In: Barer R., and Cosslett V.E. (Eds). Advances in Optical and Electron Microscopy vol. 5 (1973), Academic Press, London and New York 163-199
    • (1973) Advances in Optical and Electron Microscopy , vol.5 , pp. 163-199
    • Erickson, H.P.1
  • 15
    • 0023820449 scopus 로고
    • Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images
    • Toyoshima C., and Unwin N. Contrast transfer for frozen-hydrated specimens: determination from pairs of defocused images. Ultramicroscopy 25 4 (1988) 279-291
    • (1988) Ultramicroscopy , vol.25 , Issue.4 , pp. 279-291
    • Toyoshima, C.1    Unwin, N.2
  • 16
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • Baker T.S., Olson N.H., and Fuller S.D. Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiology and Molecular Biology Reviews 63 4 (December 1999) 862-922
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.4 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 17
    • 0002170585 scopus 로고
    • The theoretical resolution limit of the electron microscope
    • Scherzer O. The theoretical resolution limit of the electron microscope. J. Appl. Phys. 20 (January 1949) 20-29
    • (1949) J. Appl. Phys. , vol.20 , pp. 20-29
    • Scherzer, O.1
  • 20
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton W.O., and Baumeister W. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microscopy 127 (1982) 127-138
    • (1982) J. Microscopy , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 21
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Böttcher 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 6620 (1997) 88-91
    • (1997) Nature , vol.386 , Issue.6620 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 22
    • 0000167776 scopus 로고    scopus 로고
    • Appendix: measures of resolution using Fourier shell correlation
    • Appendix to Ref. [23].
    • Penczek P. Appendix: measures of resolution using Fourier shell correlation. J. Mol. Biol. 280 (1998) 115-116 Appendix to Ref. [23].
    • (1998) J. Mol. Biol. , vol.280 , pp. 115-116
    • Penczek, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.