메뉴 건너뛰기




Volumn 331, Issue 3, 2003, Pages 681-692

Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution

Author keywords

Bacterial photosynthetic reaction centre; Lipidic cubic phase crystallisation; Membrane proteins; Photosynthesis; X ray crystallography

Indexed keywords

CARDIOLIPIN; CHLORIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0043095535     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00751-4     Document Type: Article
Times cited : (112)

References (72)
  • 1
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer J., Epp O., Miki K., Huber R., Michel H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180:1984;385-398.
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 2
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors
    • Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C. Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors. Proc. Natl Acad. Sci. USA. 84:1987;5730-5734.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 5
    • 0035836485 scopus 로고    scopus 로고
    • X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: Structural changes induced by point mutations at position L209 modulate electron and proton transfer
    • Kuglstatter A., Ermler U., Michel H., Baciou L., Fritzsch G. X-ray structure analyses of photosynthetic reaction center variants from Rhodobacter sphaeroides: structural changes induced by point mutations at position L209 modulate electron and proton transfer. Biochemistry. 40:2001;4253-4260.
    • (2001) Biochemistry , vol.40 , pp. 4253-4260
    • Kuglstatter, A.1    Ermler, U.2    Michel, H.3    Baciou, L.4    Fritzsch, G.5
  • 6
    • 0037143641 scopus 로고    scopus 로고
    • Interactions between lipids and bacterial reaction centers determined by protein crystallography
    • Camara-Artigas A., Brune D., Allen J.P. Interactions between lipids and bacterial reaction centers determined by protein crystallography. Proc. Natl Acad. Sci. USA. 99:2002;11055-11060.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11055-11060
    • Camara-Artigas, A.1    Brune, D.2    Allen, J.P.3
  • 7
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • Stowell M.H., McPhillips T.M., Rees D.C., Soltis S.M., Abresch E., Feher G. Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science. 276:1997;812-816.
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 8
    • 0027176147 scopus 로고
    • New crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality
    • Buchanan S.K., Fritzsch G., Ermler U., Michel H. New crystal form of the photosynthetic reaction centre from Rhodobacter sphaeroides of improved diffraction quality. J. Mol. Biol. 230:1993;1311-1314.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1311-1314
    • Buchanan, S.K.1    Fritzsch, G.2    Ermler, U.3    Michel, H.4
  • 10
    • 0036795645 scopus 로고    scopus 로고
    • Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria
    • Fritzsch G., Koepke J., Diem R., Kuglstatter A., Baciou L. Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. Acta Crystallog. sect. D. 58:2002;1660-1663.
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 1660-1663
    • Fritzsch, G.1    Koepke, J.2    Diem, R.3    Kuglstatter, A.4    Baciou, L.5
  • 11
    • 0034671487 scopus 로고    scopus 로고
    • Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-Å resolution
    • Lancaster C.R., Bibikova M.V., Sabatino P., Oesterhelt D., Michel H. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-Å resolution. J. Biol. Chem. 275:2000;39364-39368.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39364-39368
    • Lancaster, C.R.1    Bibikova, M.V.2    Sabatino, P.3    Oesterhelt, D.4    Michel, H.5
  • 12
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:2001;909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 13
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A., Witt H., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature. 409:2001;739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 14
    • 0035927660 scopus 로고    scopus 로고
    • Structural biology. Chlorophylls galore
    • see also p. 899
    • Kuhlbrandt W. Structural biology. Chlorophylls galore. Nature. 411:2001;896-897. see also p. 899.
    • (2001) Nature , vol.411 , pp. 896-897
    • Kuhlbrandt, W.1
  • 15
    • 0016735174 scopus 로고
    • A kinetic completion of the cyclic photosynthetic electron pathway of Rhodopseudomonas sphaeroides: Cytochrome b-cytochrome c2 oxidation-reduction
    • Prince R.C., Dutton P.L. A kinetic completion of the cyclic photosynthetic electron pathway of Rhodopseudomonas sphaeroides: cytochrome b-cytochrome c2 oxidation-reduction. Biochim. Biophys. Acta. 387:1975;609-613.
    • (1975) Biochim. Biophys. Acta , vol.387 , pp. 609-613
    • Prince, R.C.1    Dutton, P.L.2
  • 16
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R., Unwin P.N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 257:1975;28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.2
  • 17
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:1990;899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 18
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L., Siegert R., Lehmann W.D., Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl Acad. Sci. USA. 95:1998;11673-11678.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 19
    • 0000095071 scopus 로고
    • Three-dimensional crystals of membrane proteins: Bacteriorhodopsin
    • Michel H., Oesterhelt D. Three-dimensional crystals of membrane proteins: bacteriorhodopsin. Proc. Natl Acad. Sci. USA. 77:1980;1283-1285.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 1283-1285
    • Michel, H.1    Oesterhelt, D.2
  • 20
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau E.M., Rosenbusch J.P. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA. 93:1996;14532-14535.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 22
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali H., Nollert P., Royant A., Menzel C., Rosenbusch J.P., Landau E.M., Pebay-Peyroula E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Struct. Fold Des. 7:1999;909-917.
    • (1999) Struct. Fold Des. , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 23
    • 0033592726 scopus 로고    scopus 로고
    • High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle
    • Edman K., Nollert P., Royant A., Belrhali H., Pebay-Peyroula E., Hajdu J., et al. High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature. 401:1999;822-826.
    • (1999) Nature , vol.401 , pp. 822-826
    • Edman, K.1    Nollert, P.2    Royant, A.3    Belrhali, H.4    Pebay-Peyroula, E.5    Hajdu, J.6
  • 25
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant A., Edman K., Ursby T., Pebay-Peyroula E., Landau E.M., Neutze R. Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature. 406:2000;645-648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E.M.5    Neutze, R.6
  • 26
    • 0034734246 scopus 로고    scopus 로고
    • Atomic resolution structures of bacteriorhodopsin photocycle intermediates: The role of discrete water molecules in the function of this light-driven ion pump
    • Luecke H. Atomic resolution structures of bacteriorhodopsin photocycle intermediates: the role of discrete water molecules in the function of this light-driven ion pump. Biochim. Biophys. Acta. 1460:2000;133-156.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 133-156
    • Luecke, H.1
  • 27
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke H., Schobert B., Richter H.T., Cartailler J.P., Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science. 286:1999;255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 28
  • 29
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass H.J., Buldt G., Gessenich R., Hehn D., Neff D., Schlesinger R., et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature. 406:2000;649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6
  • 30
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck J. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 19:2000;2152-2160.
    • (2000) EMBO J. , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 33
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution
    • Kolbe M., Besir H., Essen L.O., Oesterhelt D. Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution. Science. 288:2000;1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 34
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • Luecke H., Schobert B., Lanyi J.K., Spudich E.N., Spudich J.L. Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science. 293:2001;1499-1503.
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 36
  • 38
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 39
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstroms resolution
    • Luecke H., Richter H.T., Lanyi J.K. Proton transfer pathways in bacteriorhodopsin at 2.3 angstroms resolution. Science. 280:1998;1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 40
    • 0035979794 scopus 로고    scopus 로고
    • Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases
    • Nollert P., Qiu H., Caffrey M., Rosenbusch J.P., Landau E.M. Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases. FEBS Letters. 504:2001;179-186.
    • (2001) FEBS Letters , vol.504 , pp. 179-186
    • Nollert, P.1    Qiu, H.2    Caffrey, M.3    Rosenbusch, J.P.4    Landau, E.M.5
  • 41
    • 0015977415 scopus 로고
    • Small angle X-ray scattering of the thylakoid membranes of Rhodopseudomonas speroides in aqueous suspensions.
    • Pape E.H., Menke W., Weick D., Hosermann R. Small angle X-ray scattering of the thylakoid membranes of Rhodopseudomonas speroides in aqueous suspensions. Biophys. J. 14:1974;221-232.
    • (1974) Biophys. J. , vol.14 , pp. 221-232
    • Pape, E.H.1    Menke, W.2    Weick, D.3    Hosermann, R.4
  • 42
    • 0042109164 scopus 로고
    • Lipid analysis of cells and chromatophores of Rhodopseudomonas sphaeroides
    • Marinetti G.V., Cattieu K. Lipid analysis of cells and chromatophores of Rhodopseudomonas sphaeroides. Chem. Phys. Lipids. 28:1981;241-251.
    • (1981) Chem. Phys. Lipids , vol.28 , pp. 241-251
    • Marinetti, G.V.1    Cattieu, K.2
  • 43
    • 0023410587 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 - Membrane-protein interactions
    • Yeates T.O., Komiya H., Rees D.C., Allen J.P., Feher G. Structure of the reaction center from Rhodobacter sphaeroides R-26 - membrane-protein interactions. Proc. Natl Acad. Sci. USA. 84:1987;6438-6442.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6438-6442
    • Yeates, T.O.1    Komiya, H.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 44
    • 0019319463 scopus 로고
    • Oxidation of cytochromes c and c2 by bacterial photosynthetic reaction centers in phospholipid vesicles. 2. Studies with negative membranes
    • Overfield R.E., Wraight C.A. Oxidation of cytochromes c and c2 by bacterial photosynthetic reaction centers in phospholipid vesicles. 2. Studies with negative membranes. Biochemistry. 19:1980;3328-3334.
    • (1980) Biochemistry , vol.19 , pp. 3328-3334
    • Overfield, R.E.1    Wraight, C.A.2
  • 45
    • 0017450187 scopus 로고
    • Ubiquinone and photochemical activity in Rhodospirillum rubrum
    • Morrison L., Runquist J., Loach P. Ubiquinone and photochemical activity in Rhodospirillum rubrum. Photochem. Photobiol. 25:1977;73-84.
    • (1977) Photochem. Photobiol. , vol.25 , pp. 73-84
    • Morrison, L.1    Runquist, J.2    Loach, P.3
  • 46
    • 0027788077 scopus 로고
    • The rate of cytochrome c(2) photooxidation reflects the subcellular-distribution of reaction centers in Rhodobacter sphaeroides Ga cells
    • Vermeglio A., Joliot P., Joliot A. The rate of cytochrome c(2) photooxidation reflects the subcellular-distribution of reaction centers in Rhodobacter sphaeroides Ga cells. Biochim. Biophys. Acta. 1183:1993;352-360.
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 352-360
    • Vermeglio, A.1    Joliot, P.2    Joliot, A.3
  • 47
    • 0033603006 scopus 로고    scopus 로고
    • The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex
    • Francia F., Wang J., Venturoli G., Melandri B.A., Barz W.P., Oesterhelt D. The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex. Biochemistry. 38:1999;6834-6845.
    • (1999) Biochemistry , vol.38 , pp. 6834-6845
    • Francia, F.1    Wang, J.2    Venturoli, G.3    Melandri, B.A.4    Barz, W.P.5    Oesterhelt, D.6
  • 48
    • 0034624978 scopus 로고    scopus 로고
    • Supramolecular complexes in photosynthetic bacteria
    • Loach P.A. Supramolecular complexes in photosynthetic bacteria. Proc. Natl Acad. Sci. USA. 97:2000;5016-5018.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5016-5018
    • Loach, P.A.1
  • 49
    • 0035115358 scopus 로고    scopus 로고
    • Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?
    • Wakeham M.C., Sessions R.B., Jones M.R., Fyfe P.K. Is there a conserved interaction between cardiolipin and the type II bacterial reaction center? Biophys. J. 80:2001;1395-1405.
    • (2001) Biophys. J. , vol.80 , pp. 1395-1405
    • Wakeham, M.C.1    Sessions, R.B.2    Jones, M.R.3    Fyfe, P.K.4
  • 50
    • 0031572857 scopus 로고    scopus 로고
    • The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB
    • Lancaster C.R., Michel H. The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. Structure. 5:1997;1339-1359.
    • (1997) Structure , vol.5 , pp. 1339-1359
    • Lancaster, C.R.1    Michel, H.2
  • 51
    • 0037150088 scopus 로고    scopus 로고
    • Electrostatic interactions in an integral membrane protein
    • Johnson E.T., Parson W.W. Electrostatic interactions in an integral membrane protein. Biochemistry. 41:2002;6483-6494.
    • (2002) Biochemistry , vol.41 , pp. 6483-6494
    • Johnson, E.T.1    Parson, W.W.2
  • 52
    • 0037055974 scopus 로고    scopus 로고
    • Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria
    • Vermeglio A., Joliot P. Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria. Biochim. Biophys. Acta. 1555:2002;60-64.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 60-64
    • Vermeglio, A.1    Joliot, P.2
  • 53
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • Schneider T.R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallog. sect. D. 58:2002;195-208.
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 195-208
    • Schneider, T.R.1
  • 54
    • 0032488553 scopus 로고    scopus 로고
    • Surface pressure induced structural effects in photosynthetic reaction center Langmuir-Blodgett films
    • Facci P., Erokhin V., Paddeu S., Nicolini C. Surface pressure induced structural effects in photosynthetic reaction center Langmuir-Blodgett films. Langmuir. 14:1998;193-198.
    • (1998) Langmuir , vol.14 , pp. 193-198
    • Facci, P.1    Erokhin, V.2    Paddeu, S.3    Nicolini, C.4
  • 56
    • 0003086416 scopus 로고
    • Chemical composition and properties of reaction centers
    • R.K. Clayton, & W.R. Sistrom. New York: Plenum Press
    • Feher G., Okamura M.Y. Chemical composition and properties of reaction centers. Clayton R.K., Sistrom W.R. The Photosynthetic Bacteria. 1978;349-386 Plenum Press, New York.
    • (1978) The Photosynthetic Bacteria , pp. 349-386
    • Feher, G.1    Okamura, M.Y.2
  • 57
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 58
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza J., Saludjian P. AMoRe: an automated molecular replacement program package. Methods Enzymol. 276:1997;581-594.
    • (1997) Methods Enzymol. , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 60
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones T.A., Kjeldgaard M. Electron-density map interpretation. Methods Enzymol. 277:1997;173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 61
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 62
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 63
  • 65
    • 0034084540 scopus 로고    scopus 로고
    • Objective comparison of protein structures: Error-scaled difference distance matrices
    • Schneider T.R. Objective comparison of protein structures: error-scaled difference distance matrices. Acta Crystallog. sect. D. 56:2000;714-721.
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 714-721
    • Schneider, T.R.1
  • 66
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallog. sect. A. 32:1976;922-923.
    • (1976) Acta Crystallog. sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 67
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • see also pp. 132-134
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15:1997;112-113. see also pp. 132-134.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 112-113
    • Esnouf, R.M.1
  • 68
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+ a program for model and data visualization using persistence of vision ray-tracing
    • Fenn T.D., Ringe D., Petsko G.A. POVScript+ a program for model and data visualization using persistence of vision ray-tracing. J. Appl. Crystallog. 36:2003;944-947.
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 69
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 71
    • 0034331485 scopus 로고    scopus 로고
    • An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre
    • Ridge J.P., Fyfe P.K., McAuley K.E., van Brederode M.E., Robert B., van Grondelle R., et al. An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre. Biochem. J. 3:2000;567-578.
    • (2000) Biochem. J. , vol.3 , pp. 567-578
    • Ridge, J.P.1    Fyfe, P.K.2    McAuley, K.E.3    Van Brederode, M.E.4    Robert, B.5    Van Grondelle, R.6
  • 72
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler U., Fritzsch G., Buchanan S.K., Michel H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: cofactors and protein-cofactor interactions. Structure. 2:1994;925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.