메뉴 건너뛰기




Volumn 7, Issue 5, 2001, Pages 407-417

Accurate recording and measurement of electron diffraction data in structural and difference Fourier studies of proteins

Author keywords

Difference Fourier; Electron crystallography; Electron diffraction; Ligand binding; Protein structure; Tubulin

Indexed keywords


EID: 0039841987     PISSN: 14319276     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1431927601010406     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 0021582830 scopus 로고
    • Measurement and evaluation of electron diffraction patterns from two-dimensional crystals
    • Baldwin J, Henderson R (1984) Measurement and evaluation of electron diffraction patterns from two-dimensional crystals. Ultramicroscopy 14:319-336
    • (1984) Ultramicroscopy , vol.14 , pp. 319-336
    • Baldwin, J.1    Henderson, R.2
  • 3
    • 0028569793 scopus 로고
    • Applications of a slow-scan CCD camera in protein electron crystallography
    • Brink J, Chiu W (1994) Applications of a slow-scan CCD camera in protein electron crystallography. J Struct Biol 113:23-34
    • (1994) J Struct Biol , vol.113 , pp. 23-34
    • Brink, J.1    Chiu, W.2
  • 4
    • 0033548544 scopus 로고    scopus 로고
    • The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction
    • Bullough PA, Henderson R (1999) The projection structure of the low temperature K intermediate of the bacteriorhodopsin photocycle determined by electron diffraction. J Mol Biol 286:1663-1671
    • (1999) J Mol Biol , vol.286 , pp. 1663-1671
    • Bullough, P.A.1    Henderson, R.2
  • 5
    • 0032599786 scopus 로고    scopus 로고
    • Performance of a 2k CCD camera designed for electron crystallography at 400 kV
    • Downing KH, Hendrickson FM (1999) Performance of a 2k CCD camera designed for electron crystallography at 400 kV. Ultramicroscopy 75:215-233
    • (1999) Ultramicroscopy , vol.75 , pp. 215-233
    • Downing, K.H.1    Hendrickson, F.M.2
  • 7
    • 0032949908 scopus 로고    scopus 로고
    • Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns
    • Faruqi AR, Henderson R, Subramaniam S (1999) Cooled CCD detector with tapered fibre optics for recording electron diffraction patterns. Ultramicroscopy 75:235-250
    • (1999) Ultramicroscopy , vol.75 , pp. 235-250
    • Faruqi, A.R.1    Henderson, R.2    Subramaniam, S.3
  • 8
    • 0027724446 scopus 로고
    • High-resolution electron crystallography of protein molecules
    • Glaeser RM, Downing KH (1993) High-resolution electron crystallography of protein molecules. Ultramicroscopy 52:478-486
    • (1993) Ultramicroscopy , vol.52 , pp. 478-486
    • Glaeser, R.M.1    Downing, K.H.2
  • 9
    • 0029360316 scopus 로고
    • Diffuse scattering in electron diffraction data from protein crystals
    • Grigorieff N, Henderson R (1995) Diffuse scattering in electron diffraction data from protein crystals. Ultramicroscopy 60:295-309
    • (1995) Ultramicroscopy , vol.60 , pp. 295-309
    • Grigorieff, N.1    Henderson, R.2
  • 11
    • 0018333925 scopus 로고
    • Radiation damage of purple membrane at low temperature
    • Hayward SB, Glaeser RM (1979) Radiation damage of purple membrane at low temperature. Ultramicroscopy 4:201-210
    • (1979) Ultramicroscopy , vol.4 , pp. 201-210
    • Hayward, S.B.1    Glaeser, R.M.2
  • 12
    • 0000895319 scopus 로고
    • The difference Fourier technique in protein crystallography: Errors and their treatment
    • Henderson R, Moffat JK (1971) The difference Fourier technique in protein crystallography: errors and their treatment. Acta Crystallogr Sec B 27:1414-1420
    • (1971) Acta Crystallogr Sec B , vol.27 , pp. 1414-1420
    • Henderson, R.1    Moffat, J.K.2
  • 13
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson R, Baldwin JM, Downing KH, Lepault J, Zemlin F (1986) Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19:147-178
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 14
    • 0017476885 scopus 로고
    • Scherzer's formula and the correction of spiral distortion in the electron microscope
    • Marai FZ, Mulvey T (1977) Scherzer's formula and the correction of spiral distortion in the electron microscope. Ultramicroscopy 2:187-192
    • (1977) Ultramicroscopy , vol.2 , pp. 187-192
    • Marai, F.Z.1    Mulvey, T.2
  • 15
    • 0033605231 scopus 로고    scopus 로고
    • The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: Implication of the charge distribution
    • Mitsuoka K, Hirai T, Murata K, Miyazawa A, Kidera A, Kimura Y, Fujiyoshi Y (1999) The structure of bacteriorhodopsin at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J Mol Biol 286:861-882
    • (1999) J Mol Biol , vol.286 , pp. 861-882
    • Mitsuoka, K.1    Hirai, T.2    Murata, K.3    Miyazawa, A.4    Kidera, A.5    Kimura, Y.6    Fujiyoshi, Y.7
  • 16
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 17
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer L, Isaacs N, Bailey S (eds). Cheshire, UK: CLRC Daresbury Laboratory
    • Otwinowski Z (1993) Oscillation data reduction program. In: CCP4 Study Weekend: "Data Collection and Processing," Sawyer L, Isaacs N, Bailey S (eds). Cheshire, UK: CLRC Daresbury Laboratory, pp 56-62
    • (1993) CCP4 Study Weekend: "Data Collection and Processing," , pp. 56-62
    • Otwinowski, Z.1
  • 20
    • 0026719146 scopus 로고
    • Zero-loss energy-filtered imaging of frozen-hydrated proteins: Model calculations and implications for future developments
    • Schröder RR (1992) Zero-loss energy-filtered imaging of frozen-hydrated proteins: model calculations and implications for future developments. J Microsc 166:389-400
    • (1992) J Microsc , vol.166 , pp. 389-400
    • Schröder, R.R.1
  • 21
    • 0033386253 scopus 로고    scopus 로고
    • Electron crystallography of bacteriorhodopsin with millisecond time resolution
    • Subramaniam S, Henderson R (1999) Electron crystallography of bacteriorhodopsin with millisecond time resolution. J Struct Biol 128:19-25
    • (1999) J Struct Biol , vol.128 , pp. 19-25
    • Subramaniam, S.1    Henderson, R.2
  • 22
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin PNT, Henderson R (1975) Molecular structure determination by electron microscopy of unstained crystalline specimens. J Mol Biol 94:425-440
    • (1975) J Mol Biol , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 23
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck J (2000) Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J 19: 2152-2160
    • (2000) EMBO J , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 24
    • 4243672210 scopus 로고
    • Microdensitometry applied to X-ray photographs
    • Wooster WA (1964) Microdensitometry applied to X-ray photographs. Acta Crystallogr 17:878-882
    • (1964) Acta Crystallogr , vol.17 , pp. 878-882
    • Wooster, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.