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Volumn 128, Issue 1, 1999, Pages 44-50

Haloarcula marismortui 50S subunit - Complementarity of electron microscopy and X-ray crystallographic information

Author keywords

Cryo electron microscopy; X ray crystallography

Indexed keywords

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; FOURIER ANALYSIS; INTERMETHOD COMPARISON; OPTICAL RESOLUTION; PRIORITY JOURNAL; RIBOSOME SUBUNIT; X RAY CRYSTALLOGRAPHY;

EID: 0033396635     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1999.4157     Document Type: Article
Times cited : (17)

References (19)
  • 1
    • 0032967391 scopus 로고    scopus 로고
    • Conformational variability in E. coli 70S ribosome as revealed by 3D cryo-electron microscopy
    • Agrawal R. K., Lata K. R., Frank J. Conformational variability in E. coli 70S ribosome as revealed by 3D cryo-electron microscopy. Int. J. Biochem. Cell Biol. 31:1999;243-254.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 243-254
    • Agrawal, R.K.1    Lata, K.R.2    Frank, J.3
  • 4
    • 0015672282 scopus 로고
    • The envelope function of electron microscopic transfer function for partially coherent illumination
    • Frank J. The envelope function of electron microscopic transfer function for partially coherent illumination. Optik. 38:1973;519-536.
    • (1973) Optik , vol.38 , pp. 519-536
    • Frank, J.1
  • 5
    • 0000676323 scopus 로고
    • On the correction of the contrast transfer function in biological electron microscopy
    • Frank J., Penczek P. On the correction of the contrast transfer function in biological electron microscopy. Optik. 98:1995;125-129.
    • (1995) Optik , vol.98 , pp. 125-129
    • Frank, J.1    Penczek, P.2
  • 7
    • 0026664623 scopus 로고
    • Bacteriophage phi 6 envelope elucidated by chemical cross-linking, immunodetection, and cryoelectron microscopy
    • Kenney J. M., Hantula J., Fuller S. D., Mindich L., Ojala P. M., Bamford D. H. Bacteriophage phi 6 envelope elucidated by chemical cross-linking, immunodetection, and cryoelectron microscopy. Virology. 190:1992;635-644.
    • (1992) Virology , vol.190 , pp. 635-644
    • Kenney, J.M.1    Hantula, J.2    Fuller, S.D.3    Mindich, L.4    Ojala, P.M.5    Bamford, D.H.6
  • 9
    • 0026533909 scopus 로고
    • Inter-protein distances within the large subunit from Escherichia coli ribosomes
    • May R. P., Nowotny V., Nowotny P., Voss H., Nierhaus K. H. Inter-protein distances within the large subunit from Escherichia coli ribosomes. EMBO J. 11:1992;373-378.
    • (1992) EMBO J. , vol.11 , pp. 373-378
    • May, R.P.1    Nowotny, V.2    Nowotny, P.3    Voss, H.4    Nierhaus, K.H.5
  • 10
    • 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., 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
  • 11
    • 0030198739 scopus 로고    scopus 로고
    • A common-lines based method for determining orientations for N > 3 particle projections simultaneously
    • Penczek P. A., Zhu J., Frank J. A common-lines based method for determining orientations for N > 3 particle projections simultaneously. Ultramicroscopy. 63:1996;205-218.
    • (1996) Ultramicroscopy , vol.63 , pp. 205-218
    • Penczek, P.A.1    Zhu, J.2    Frank, J.3
  • 12
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial envelope protein
    • Saxton W. O., Baumeister W. The correlation averaging of a regularly arranged bacterial envelope protein. J. Microsc. 127:1982;127-138.
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 15
    • 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
  • 16
    • 0017541997 scopus 로고
    • Electron microscope transfer function for partially coherent axial illumination and chromatic defocus spread
    • Wade R. H., Frank J. Electron microscope transfer function for partially coherent axial illumination and chromatic defocus spread. Optik. 49:1977;81-92.
    • (1977) Optik , vol.49 , pp. 81-92
    • Wade, R.H.1    Frank, J.2
  • 17
    • 0001836114 scopus 로고
    • Ribosomal proteins: Their structure and evolution
    • B. Hardesty, & G. Kramer. New York: Springer-Verlag
    • Wittman-Liebold B. Ribosomal proteins: Their structure and evolution. Hardesty B., Kramer G. Structure, Function, and Genetics of Ribosomes. 1986;326-361 Springer-Verlag, New York.
    • (1986) Structure, Function, and Genetics of Ribosomes , pp. 326-361
    • Wittman-Liebold, B.1
  • 19
    • 0030960710 scopus 로고    scopus 로고
    • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: Procedure and application to the 70S Escherichia coli ribosome
    • Zhu J., Penczek P. A., Schröder R., Frank J. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: Procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 118:1997;197-219.
    • (1997) J. Struct. Biol. , vol.118 , pp. 197-219
    • Zhu, J.1    Penczek, P.A.2    Schröder, R.3    Frank, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.