메뉴 건너뛰기




Volumn 4, Issue 5, 1996, Pages 581-597

The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum

Author keywords

Bacteriochlorophyll; Dexter energy transfer; F rster exciton transfer mechanism; Membrane protein; Photosynthesis; X ray crystallography

Indexed keywords

BACTERIA (MICROORGANISMS); PHAEOSPIRILLUM MOLISCHIANUM; PROTEOBACTERIA; RHODOBLASTUS ACIDOPHILUS; RHODOPSEUDOMONAS; RHODOSPIRILLUM;

EID: 0030585121     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00063-9     Document Type: Article
Times cited : (998)

References (74)
  • 1
    • 0001151569 scopus 로고
    • Structure and function of light-harvesting complexes and their polypeptides
    • Zuber, H. (1985). Structure and function of light-harvesting complexes and their polypeptides. Photochem. Photobiol. 42, 821-825.
    • (1985) Photochem. Photobiol. , vol.42 , pp. 821-825
    • Zuber, H.1
  • 2
    • 0343100946 scopus 로고
    • Structural features of photosynthetic light-harvesting systems
    • Deisenhofer, J. & Norris, J.R., eds, Academic Press, San Diego
    • Zuber, H. (1993). Structural features of photosynthetic light-harvesting systems. In The Photosynthetic Reaction Center. (Deisenhofer, J. & Norris, J.R., eds), pp. 43-100, Academic Press, San Diego.
    • (1993) The Photosynthetic Reaction Center , pp. 43-100
    • Zuber, H.1
  • 3
    • 0028953308 scopus 로고
    • 8.5 Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits
    • Karrasch, S., Bullough, P. & Ghosh, R. (1995). 8.5 Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO J. 14, 631-638.
    • (1995) EMBO J. , vol.14 , pp. 631-638
    • Karrasch, S.1    Bullough, P.2    Ghosh, R.3
  • 5
    • 18244397526 scopus 로고
    • A theory of sensitized luminescence in solids
    • Dexter, D. (1953). A theory of sensitized luminescence in solids. J. Chem. Phys. 21, 836-850.
    • (1953) J. Chem. Phys. , vol.21 , pp. 836-850
    • Dexter, D.1
  • 7
    • 0020632373 scopus 로고
    • The isolation and partial characterization of the light-harvesting pigment-protein complement of Rhodopseudomonas acidophila
    • Cogdell, R.J., Durant, I., Valentine, J., Lindsay, J.G. & Schmidt, K. (1983). The isolation and partial characterization of the light-harvesting pigment-protein complement of Rhodopseudomonas acidophila. Biochim. Biophys. Acta 722, 427-455.
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 427-455
    • Cogdell, R.J.1    Durant, I.2    Valentine, J.3    Lindsay, J.G.4    Schmidt, K.5
  • 8
    • 0021802669 scopus 로고
    • Crystallization of the photosynthetic light-harvesting pigment-protein complex B800-850 of Rhodopseudomonas capsulata
    • Weite, W., et al., & Drews, G. (1985). Crystallization of the photosynthetic light-harvesting pigment-protein complex B800-850 of Rhodopseudomonas capsulata. FEBS Lett. 182, 260-264.
    • (1985) FEBS Lett. , vol.182 , pp. 260-264
    • Weite, W.1    Drews, G.2
  • 9
    • 0022553138 scopus 로고
    • Crystallization and spectroscopic investigation with polarized light of the reaction center-B875 light-harvesting complex of Rhodopseudomonas palustris
    • Wacker, T., et al., & Weite, W. (1986). Crystallization and spectroscopic investigation with polarized light of the reaction center-B875 light-harvesting complex of Rhodopseudomonas palustris. FEBS Lett. 197, 267-273.
    • (1986) FEBS Lett. , vol.197 , pp. 267-273
    • Wacker, T.1    Weite, W.2
  • 10
    • 0024358023 scopus 로고
    • Crystallization of two crystal forms of the B800-850 light-harvesting complex from Rhodopseudomonas acidophila strain 10050
    • Papiz, M.Z., et al., & Lindsay, J.G. (1989). Crystallization of two crystal forms of the B800-850 light-harvesting complex from Rhodopseudomonas acidophila strain 10050. J. Mol. Biol. 209, 833-835.
    • (1989) J. Mol. Biol. , vol.209 , pp. 833-835
    • Papiz, M.Z.1    Lindsay, J.G.2
  • 11
    • 85143328503 scopus 로고
    • General and practical aspects of membrane protein crystallization
    • Michel, H., ed, CRC Press, Boca Raton, FL
    • Michel, H. (1991). General and practical aspects of membrane protein crystallization. In Crystallization of Membrane Proteins. (Michel, H., ed), pp. 74-88, CRC Press, Boca Raton, FL.
    • (1991) Crystallization of Membrane Proteins , pp. 74-88
    • Michel, H.1
  • 12
    • 0027263521 scopus 로고
    • Two-dimensional crystallization of the light-harvesting complex from Rhodospirillum rubrum
    • 2. Ghosh, R., et al., & Rosenbusch, J.P. (1993). Two-dimensional crystallization of the light-harvesting complex from Rhodospirillum rubrum. J. Mol. Biol. 231, 501-504.
    • (1993) J. Mol. Biol. , vol.231 , pp. 501-504
    • Ghosh, R.1    Rosenbusch, J.P.2
  • 13
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1985). Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution. Nature 318, 618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 14
    • 0005384356 scopus 로고
    • The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J. & Michel, H. (1989). The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8, 2149-2170.
    • (1989) EMBO J. , vol.8 , pp. 2149-2170
    • Deisenhofer, J.1    Michel, H.2
  • 15
    • 0024157070 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: Symmetry relations and sequence comparison between different species
    • Komiya, H., Yeates, T.O., Rees, D.C., Allen, J.P. & Feher, G. (1988). Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparison between different species. Proc. Natl. Acad. Sci. USA 85, 9012-9016.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9012-9016
    • Komiya, H.1    Yeates, T.O.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 16
    • 0025784505 scopus 로고
    • Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang, C.-H., El-Kabbani, O., Tiede, D., Norris, J. & Schiffer, M. (1991). Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 30, 5352-5360.
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.-H.1    El-Kabbani, O.2    Tiede, D.3    Norris, J.4    Schiffer, M.5
  • 17
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: Cofactors and protein-cofactor interactions
    • Ermler, U., Fritzsch, G., Buchanan, S. K. & Michel, H. (1994). Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. Structure 2, 925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 18
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D.-N. & Fujiyoshi, Y. (1994). Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.-N.2    Fujiyoshi, Y.3
  • 19
    • 0029029180 scopus 로고
    • Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum
    • Montoya, G., Cyrklaff, M. & Sinning, I. (1995). Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. J. Mol. Biol. 250, 1-10.
    • (1995) J. Mol. Biol. , vol.250 , pp. 1-10
    • Montoya, G.1    Cyrklaff, M.2    Sinning, I.3
  • 20
    • 0029637583 scopus 로고
    • Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria
    • McDermott, G., et al., & Isaacs, N. (1995). Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374, 517-521.
    • (1995) Nature , vol.374 , pp. 517-521
    • McDermott, G.1    Isaacs, N.2
  • 21
    • 0027195504 scopus 로고
    • Unexpected similarities of the B800-850 light-harvesting complex from Rhodospirillum molischianum to the B870 light-harvesting complexes from other purple photosynthetic bacteria
    • Germeroth, L., Lottspeich, F., Robert, B. & Michel, H. (1993). Unexpected similarities of the B800-850 light-harvesting complex from Rhodospirillum molischianum to the B870 light-harvesting complexes from other purple photosynthetic bacteria. Biochemistry 32, 5615-5621.
    • (1993) Biochemistry , vol.32 , pp. 5615-5621
    • Germeroth, L.1    Lottspeich, F.2    Robert, B.3    Michel, H.4
  • 22
    • 0029153599 scopus 로고
    • Predicting the structure of the light-harvesting complex II of Rhodospirillum molischianum
    • Hu, X., Xu, D., Hamer, K., Schulten, K., Koepke, J. & Michel, H. (1995). Predicting the structure of the light-harvesting complex II of Rhodospirillum molischianum. Protein Sci. 4, 1670-1682.
    • (1995) Protein Sci. , vol.4 , pp. 1670-1682
    • Hu, X.1    Xu, D.2    Hamer, K.3    Schulten, K.4    Koepke, J.5    Michel, H.6
  • 25
    • 0026088998 scopus 로고
    • The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles
    • Timmins, P.A., Hauk, J., Wacker, T. & Weite, W. (1991). The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles. FEBS Lett. 280, 115-120.
    • (1991) FEBS Lett. , vol.280 , pp. 115-120
    • Timmins, P.A.1    Hauk, J.2    Wacker, T.3    Weite, W.4
  • 26
    • 0027958751 scopus 로고
    • Determination of the number of detergent molecules associated with the reaction centre from Rhodopseudomonas viridis
    • Gast, P., Hemelrijk, P. & Hoff, A.J. (1994). Determination of the number of detergent molecules associated with the reaction centre from Rhodopseudomonas viridis. FEBS Lett. 337, 39-42.
    • (1994) FEBS Lett. , vol.337 , pp. 39-42
    • Gast, P.1    Hemelrijk, P.2    Hoff, A.J.3
  • 27
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of error in these models
    • Jones, A., Zou, J.-Y., Cowan, S. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of error in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 29
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzati, V. (1952). Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Cryst. 5, 802-810.
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 31
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 335, 472-474.
    • (1992) Nature , vol.335 , pp. 472-474
    • Brünger, A.T.1
  • 32
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brünger, AT. (1993). Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Cryst. D 49, 24-36.
    • (1993) Acta Cryst. D , vol.49 , pp. 24-36
    • Brünger, A.T.1
  • 33
    • 0011221526 scopus 로고    scopus 로고
    • Good model-building and refinement practice
    • in press
    • Kleywegt, G.J. & Jones, T.A. (1996). Good model-building and refinement practice. Methods Enzymol., in press.
    • (1996) Methods Enzymol.
    • Kleywegt, G.J.1    Jones, T.A.2
  • 34
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-transretinoic acid and a synthetic retinoid
    • Kleywegt, G.J., et al., & Jones, T.A. (1994). Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-transretinoic acid and a synthetic retinoid. Structure 2, 1241-1258.
    • (1994) Structure , vol.2 , pp. 1241-1258
    • Kleywegt, G.J.1    Jones, T.A.2
  • 35
    • 0016766522 scopus 로고
    • Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola
    • Fenna, R.E. & Matthews, B.W. (1975). Chlorophyll arrangement in a bacteriochlorophyll protein from Chlorobium limicola. Nature 258, 573-577.
    • (1975) Nature , vol.258 , pp. 573-577
    • Fenna, R.E.1    Matthews, B.W.2
  • 36
    • 0018333224 scopus 로고
    • Structure of a bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii
    • Matthews, B.W., Fenna, R.E., Bolognesi, M.C., Schmid, M.F. & Olson, J.M. (1979). Structure of a bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii. J. Mol. Biol. 131, 259-285.
    • (1979) J. Mol. Biol. , vol.131 , pp. 259-285
    • Matthews, B.W.1    Fenna, R.E.2    Bolognesi, M.C.3    Schmid, M.F.4    Olson, J.M.5
  • 37
    • 0023042001 scopus 로고
    • Structure and X-ray amino acid sequence of a bacteriochlorophyll-a protein from Prosthecochloris aestuarii refined at 1.9 A resolution
    • Tronrud, D.E., Schmid, M.F. & Matthews, B.W. (1986). Structure and X-ray amino acid sequence of a bacteriochlorophyll-a protein from Prosthecochloris aestuarii refined at 1.9 A resolution. J. Mol. Biol. 188, 443-454.
    • (1986) J. Mol. Biol. , vol.188 , pp. 443-454
    • Tronrud, D.E.1    Schmid, M.F.2    Matthews, B.W.3
  • 38
    • 0023483526 scopus 로고
    • How carotenoids function in photosynthetic bacteria
    • Cogdell, R. & Frank, H. (1987). How carotenoids function in photosynthetic bacteria. Biochim. Biophys. Acta 895, 63-79.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 63-79
    • Cogdell, R.1    Frank, H.2
  • 39
    • 0015386420 scopus 로고
    • Unambiguous evidence for the participation of singlet oxygen (1) in photodynamic oxidation of amino acids
    • Nilsson, R., Merkel, P. & Kearns, D. (1972). Unambiguous evidence for the participation of singlet oxygen (1) in photodynamic oxidation of amino acids. Photochem. Photobiol. 16, 117-124.
    • (1972) Photochem. Photobiol. , vol.16 , pp. 117-124
    • Nilsson, R.1    Merkel, P.2    Kearns, D.3
  • 40
    • 84989729939 scopus 로고
    • Absorption spectral shifts of carotenoids related to medium polarizability
    • Anderson, P., Gillbro, T., Ferguson, L. & Cogdell, R. (1991). Absorption spectral shifts of carotenoids related to medium polarizability. Photochem. Photobiol. 54, 353-360.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 353-360
    • Anderson, P.1    Gillbro, T.2    Ferguson, L.3    Cogdell, R.4
  • 41
    • 85143331539 scopus 로고
    • Detergent phenomena in membrane protein crystallization
    • Michel, H., ed, CRC Press, Boca Raton, FL
    • Zulauf, M. (1991). Detergent phenomena in membrane protein crystallization. In Crystallization of Membrane Proteins. (Michel, H., ed), pp. 53-72, CRC Press, Boca Raton, FL.
    • (1991) Crystallization of Membrane Proteins , pp. 53-72
    • Zulauf, M.1
  • 42
    • 36849148472 scopus 로고
    • Detergent structure in crystals of a bacterial photosynthetic reaction center
    • Roth, M., Lewit-Bentley, A., Michel, H., Deisenhofer, J., Huber, R. & Oesterhelt, D. (1989). Detergent structure in crystals of a bacterial photosynthetic reaction center. Nature 340, 659-662.
    • (1989) Nature , vol.340 , pp. 659-662
    • Roth, M.1    Lewit-Bentley, A.2    Michel, H.3    Deisenhofer, J.4    Huber, R.5    Oesterhelt, D.6
  • 43
    • 1542432461 scopus 로고    scopus 로고
    • Dynamics in isolated bacterial light harvesting antenna (LH2) of Rhodobacter sphaeroides at room temperature
    • Joo, T., Jia, Y., Yu, J.-Y., Jonas, D. & Fleming, G. (1996). Dynamics in isolated bacterial light harvesting antenna (LH2) of Rhodobacter sphaeroides at room temperature. J. Chem. Phys. 100, 2399-2409.
    • (1996) J. Chem. Phys. , vol.100 , pp. 2399-2409
    • Joo, T.1    Jia, Y.2    Yu, J.-Y.3    Jonas, D.4    Fleming, G.5
  • 44
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster, T. (1948). Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. NY 2, 55-75.
    • (1948) Ann. Phys. NY , vol.2 , pp. 55-75
    • Förster, T.1
  • 45
    • 0042813364 scopus 로고
    • Spectra of porphyrins
    • Gouterman, M. (1961). Spectra of porphyrins. J. Mol. Spectrosc. 6, 138-163.
    • (1961) J. Mol. Spectrosc. , vol.6 , pp. 138-163
    • Gouterman, M.1
  • 46
    • 0002184931 scopus 로고
    • The Pi electron structure and absorption spectra of chlorophylls in solution
    • Weiss, C. (1972). The Pi electron structure and absorption spectra of chlorophylls in solution. J. Mol. Spectrosc. 44, 37-80.
    • (1972) J. Mol. Spectrosc. , vol.44 , pp. 37-80
    • Weiss, C.1
  • 47
  • 48
    • 0041520204 scopus 로고
    • Spectroscopic determinants in the reaction center of Rhodopseudomonas viridis. Biophys
    • Eccles, J., Honig, B. & Schulten, K. (1988). Spectroscopic determinants in the reaction center of Rhodopseudomonas viridis. Biophys. J. 53, 137-144.
    • (1988) J. , vol.53 , pp. 137-144
    • Eccles, J.1    Honig, B.2    Schulten, K.3
  • 50
    • 0002908796 scopus 로고
    • Exciton states and energy transfer in bacterial membranes: The role of pigment-protein cyclic unit structure
    • Michel-Beyerle, M., ed, Springer-Verlag, Berlin
    • Pearlstein, R. & Zuber, H. (1985). Exciton states and energy transfer in bacterial membranes: the role of pigment-protein cyclic unit structure. In Antennas and Reaction Centers of Photosynthetic Bacteria. (Michel-Beyerle, M., ed), pp. 53-61, Springer-Verlag, Berlin.
    • (1985) Antennas and Reaction Centers of Photosynthetic Bacteria , pp. 53-61
    • Pearlstein, R.1    Zuber, H.2
  • 51
    • 0028934513 scopus 로고
    • Exciton dynamics in circular aggregates: Application to antenna of photosynthetic purple bacteria
    • Novoderezhkin, V. & Razjivin, A. (1995). Exciton dynamics in circular aggregates: application to antenna of photosynthetic purple bacteria. Biophys. J. 68, 1089-1100.
    • (1995) Biophys. J. , vol.68 , pp. 1089-1100
    • Novoderezhkin, V.1    Razjivin, A.2
  • 52
    • 10644259457 scopus 로고    scopus 로고
    • Prediction of the Structure of an Integral Membrane Protein - The Light-Harvesting Complex II of Rhodospirillum molischianum
    • Merz, K. & Roux, B., eds, Birkhäuser, Cambridge, MA, in press
    • Hu, X., Xu, D., Hamer, K., Schulten, K., Koepke, J. & Michel, H. (1996). Prediction of the Structure of an Integral Membrane Protein - The Light-Harvesting Complex II of Rhodospirillum molischianum. In Biological Membranes: A Molecular Perspective from Computation and Experiment. (Merz, K. & Roux, B., eds, Birkhäuser, Cambridge, MA, in press.
    • (1996) Biological Membranes: A Molecular Perspective from Computation and Experiment
    • Hu, X.1    Xu, D.2    Hamer, K.3    Schulten, K.4    Koepke, J.5    Michel, H.6
  • 53
    • 85005726073 scopus 로고
    • Directed mutations affecting the putative bacteriochlorophyll-binding sites in the light-harvesting I antenna of Rhodobacter capsulatus
    • Bylina, E., Robles, S. & Youvan, D. (1988). Directed mutations affecting the putative bacteriochlorophyll-binding sites in the light-harvesting I antenna of Rhodobacter capsulatus. Isr. J. Chem. 28, 73-78.
    • (1988) Isr. J. Chem. , vol.28 , pp. 73-78
    • Bylina, E.1    Robles, S.2    Youvan, D.3
  • 54
    • 0028008899 scopus 로고
    • Probing the B800 bacteriochlorophyll binding site of the accessory light-harvesting complex from Rhodobacter sphaeroides using site-directed mutants. I. Mutagenesis, effects on binding, function and electrochromic behaviour of its carotenoids
    • Crielaard, W., Visschers, R., Fowler, G., van Grondelle, R., Hellingwerf, K., & Hunter, C. (1994). Probing the B800 bacteriochlorophyll binding site of the accessory light-harvesting complex from Rhodobacter sphaeroides using site-directed mutants. I. Mutagenesis, effects on binding, function and electrochromic behaviour of its carotenoids. Biochim. Biophys. Acta 1183, 473-482.
    • (1994) Biochim. Biophys. Acta , vol.1183 , pp. 473-482
    • Crielaard, W.1    Visschers, R.2    Fowler, G.3    Van Grondelle, R.4    Hellingwerf, K.5    Hunter, C.6
  • 55
    • 0001485575 scopus 로고
    • Structure of light-harvesting antenna complexes of photosynthetic bacteria, cyanobacteria and red algae
    • Zuber, H. (1986). Structure of light-harvesting antenna complexes of photosynthetic bacteria, cyanobacteria and red algae. Trends Biochem. Sci. 11, 414-419.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 414-419
    • Zuber, H.1
  • 56
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • Schiffer, M., Chang, C.-H. & Stevens, F. J. (1992). The functions of tryptophan residues in membrane proteins. Protein Eng. 5, 213-214.
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 57
    • 0000693357 scopus 로고
    • Excitation energy transfer in photosynthesis
    • Scheer, H., ed, Walter de Gruyter & Co, Berlin, NY
    • van Grondelle, R. & Sundstrom, V. (1988). Excitation energy transfer in photosynthesis. In Photosynthetic Light-Harvesting Systems. (Scheer, H., ed), pp. 403-438, Walter de Gruyter & Co, Berlin, NY.
    • (1988) Photosynthetic Light-Harvesting Systems , pp. 403-438
    • Van Grondelle, R.1    Sundstrom, V.2
  • 58
    • 0002452464 scopus 로고
    • Oscillation Data Reduction Program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation Data Reduction Program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 60
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computer Project No. 4.
    • Collaborative Computer Project No. 4. (1994). The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 61
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T.L. (1993). Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 63
    • 0029633187 scopus 로고
    • MDScope - A Visual Computing Environment for Structural Biology
    • Nelson, M., et al., & Kufrin, R. (1995). MDScope - A Visual Computing Environment for Structural Biology. Comput. Phys. Commun. 91, 111-134.
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 111-134
    • Nelson, M.1    Kufrin, R.2
  • 64
    • 0022335493 scopus 로고
    • Diffraction methods for biological macromolecules. Use of the rotation and translation functions
    • Lattman, E. (1985). Diffraction methods for biological macromolecules. Use of the rotation and translation functions. Methods Enzymol. 115, 55-77.
    • (1985) Methods Enzymol. , vol.115 , pp. 55-77
    • Lattman, E.1
  • 66
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger, AT. (1990). Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Cryst. A 46, 46-57.
    • (1990) Acta Cryst. A , vol.46 , pp. 46-57
    • Brünger, A.T.1
  • 67
    • 0001557614 scopus 로고
    • On integrating the techniques of direct methods and isomorphous replacement. I. The theoretical basis
    • Hauptman, H. (1982). On integrating the techniques of direct methods and isomorphous replacement. I. The theoretical basis. Acta Cryst. A 38, 289-294.
    • (1982) Acta Cryst. A , vol.38 , pp. 289-294
    • Hauptman, H.1
  • 68
    • 0002700643 scopus 로고
    • Halloween... Masks and Bones
    • Bailey, S., Hubbard, R. & Waller, D., eds, SERC Daresbury Laboratory, Warrington, UK
    • Kleywegt, G.J. & Jones, A.T. (1994). Halloween... Masks and Bones. In Proceedings of the CCP4 Study Weekend: From First Map to Final Model, (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 59-66, SERC Daresbury Laboratory, Warrington, UK.
    • (1994) Proceedings of the CCP4 Study Weekend: From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, A.T.2
  • 69
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 72
    • 0002552477 scopus 로고
    • A set of averaging programs
    • a, yaap, asap, @#*? Dodson, E.J., Glover, S. & Wolf, W., eds, SERC Daresbury Laboratory, Warrington, UK
    • Jones, T.A. (1992). a, yaap, asap, @#*? A set of averaging programs. In Proceedings of the CCP4 Study Weekend: Molecular Replacement. (Dodson, E.J., Glover, S. & Wolf, W., eds), pp. 92-105, SERC Daresbury Laboratory, Warrington, UK.
    • (1992) Proceedings of the CCP4 Study Weekend: Molecular Replacement , pp. 92-105
    • Jones, T.A.1
  • 73
    • 0030608154 scopus 로고    scopus 로고
    • Molecular cloning, DNA sequence and transcription analysis of the Rhodospirillum molischianum B800/850 light-harvesting genes
    • in press
    • Germeroth, L., Reiländer, H. & Michel, H. (1996). Molecular cloning, DNA sequence and transcription analysis of the Rhodospirillum molischianum B800/850 light-harvesting genes. Biochim. Biophys. Acta, in press.
    • (1996) Biochim. Biophys. Acta
    • Germeroth, L.1    Reiländer, H.2    Michel, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.