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Volumn 75, Issue 1, 1998, Pages 255-263

Sulfur distribution in bacteriorhodopsin from multiple wavelength anomalous diffraction near the sulfur K-edge with synchrotron x-ray radiation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; SULFUR;

EID: 0031863432     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77512-5     Document Type: Article
Times cited : (15)

References (36)
  • 2
    • 85030336161 scopus 로고    scopus 로고
    • X-ray diffraction studies on bacteriorhodopsin: Localization of loop- and sulfur-containing residues
    • Behrens, W., H. Otto, R. Mollaaghababa, U. Alexiev, H. G. Khorana, and M. P. Heyn. 1997. X-ray diffraction studies on bacteriorhodopsin: localization of loop-and sulfur-containing residues. Biophys. J. 72:A208.
    • (1997) Biophys. J. , vol.72
    • Behrens, W.1    Otto, H.2    Mollaaghababa, R.3    Alexiev, U.4    Khorana, H.G.5    Heyn, M.P.6
  • 3
    • 0024033744 scopus 로고
    • Data acquisition systems for linear and area x-ray detectors using delay line readout
    • Boulin, C. J., R. Kempf, A. Gabriel, and M. H. J. Koch. 1988. Data acquisition systems for linear and area x-ray detectors using delay line readout. Nucl. Instrum. Methods. A269:312-320.
    • (1988) Nucl. Instrum. Methods , vol.A269 , pp. 312-320
    • Boulin, C.J.1    Kempf, R.2    Gabriel, A.3    Koch, M.H.J.4
  • 4
    • 0344933349 scopus 로고
    • X-ray diffraction studies of the stretching and relaxing of polyethylene
    • Brown, A. 1949. X-ray diffraction studies of the stretching and relaxing of polyethylene. J. Appl. Phys. 20:552-558.
    • (1949) J. Appl. Phys. , vol.20 , pp. 552-558
    • Brown, A.1
  • 7
    • 0002090350 scopus 로고
    • Analysis of macromolecular structures by the method of multiwavelength anomalous diffraction
    • S. S. Hasnain, editor. Harwood Publishers, Chichester
    • Fourme, R., and W. A. Hendrickson. 1990. Analysis of macromolecular structures by the method of multiwavelength anomalous diffraction. In Synchrotron Radiation and Biophysics. S. S. Hasnain, editor. Harwood Publishers, Chichester. 156-175.
    • (1990) Synchrotron Radiation and Biophysics , pp. 156-175
    • Fourme, R.1    Hendrickson, W.A.2
  • 8
    • 0017539686 scopus 로고
    • Position sensitive x-ray detector
    • Gabriel, A. 1977. Position sensitive x-ray detector. Rev. Sci. Instrum. 48:1303-1305.
    • (1977) Rev. Sci. Instrum. , vol.48 , pp. 1303-1305
    • Gabriel, A.1
  • 9
    • 0022407354 scopus 로고
    • Structural comparison of native and deoxycholate treated purple membrane
    • Glaeser, R. M., J. S. Jubb, and R. Henderson. 1985. Structural comparison of native and deoxycholate treated purple membrane. Biophys. J. 48: 775-780.
    • (1985) Biophys. J. , vol.48 , pp. 775-780
    • Glaeser, R.M.1    Jubb, J.S.2    Henderson, R.3
  • 10
  • 11
    • 0025300323 scopus 로고
    • Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction
    • Hauss, T., S. Grzesiek, H. Otto, J. Westerhausen, and M. P. Heyn. 1990. Transmembrane location of retinal in bacteriorhodopsin by neutron diffraction. Biochemistry. 29:4904-4913.
    • (1990) Biochemistry , vol.29 , pp. 4904-4913
    • Hauss, T.1    Grzesiek, S.2    Otto, H.3    Westerhausen, J.4    Heyn, M.P.5
  • 13
    • 0025071357 scopus 로고
    • Cryo-protection of protein crystals against radiation damage in electron and x-ray diffraction
    • Henderson, R. 1990. Cryo-protection of protein crystals against radiation damage in electron and x-ray diffraction. Proc. R. Soc. Lond. Biol. 241:6-8.
    • (1990) Proc. R. Soc. Lond. Biol. , vol.241 , pp. 6-8
    • Henderson, R.1
  • 14
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 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
  • 15
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson, W. A. 1991. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254: 51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 16
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson, W. A., J. R. Horton, and D. M. Le Master. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Le Master, D.M.3
  • 17
    • 0019450355 scopus 로고
    • Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur
    • Hendrickson, W. A., and M. M. Teeter. 1981. Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature. 290:107-113.
    • (1981) Nature , vol.290 , pp. 107-113
    • Hendrickson, W.A.1    Teeter, M.M.2
  • 18
    • 0039126842 scopus 로고
    • Anomalous scattering and the phase problem
    • Herzenberg, A., and H. S. M. Lau. 1967. Anomalous scattering and the phase problem. Acta Crystallogr. 22:24-28.
    • (1967) Acta Crystallogr. , vol.22 , pp. 24-28
    • Herzenberg, A.1    Lau, H.S.M.2
  • 19
    • 0024121506 scopus 로고
    • High sensitivity neutron diffraction of membranes: Location of the Schiff base end of the chromophore of bacteriorhodopsin
    • Heyn, M. P., J. Westerhausen, I. Wallat, and F. Seiff. 1989. High sensitivity neutron diffraction of membranes: location of the Schiff base end of the chromophore of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 85:2146-2150.
    • (1989) Proc. Natl. Acad. Sci. USA. , vol.85 , pp. 2146-2150
    • Heyn, M.P.1    Westerhausen, J.2    Wallat, I.3    Seiff, F.4
  • 21
    • 21244499919 scopus 로고
    • Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
    • Kates, M., S. C. Kushwaha, and G. D. Sprott. 1982. Lipids of purple membrane from extreme halophiles and of methanogenic bacteria. Methods Enzymol. 80:98-111.
    • (1982) Methods Enzymol. , vol.80 , pp. 98-111
    • Kates, M.1    Kushwaha, S.C.2    Sprott, G.D.3
  • 22
    • 0025976082 scopus 로고
    • Time-resolved x-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin
    • Koch, M. H. J., N. A. Dencher, D. Oesterhelt, H.-J. Plöhn, G. Rapp, and G. Büldt. 1991. Time-resolved x-ray diffraction study of structural changes associated with the photocycle of bacteriorhodopsin. EMBO J. 10: 521-526.
    • (1991) EMBO J. , vol.10 , pp. 521-526
    • Koch, M.H.J.1    Dencher, N.A.2    Oesterhelt, D.3    Plöhn, H.-J.4    Rapp, G.5    Büldt, G.6
  • 23
    • 0027141461 scopus 로고
    • X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane protein
    • Krebs, M. P., W. Behrens, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn. 1993. X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane protein. Biochemistry. 32:12830-12834.
    • (1993) Biochemistry , vol.32 , pp. 12830-12834
    • Krebs, M.P.1    Behrens, W.2    Mollaaghababa, R.3    Khorana, H.G.4    Heyn, M.P.5
  • 24
    • 0026506038 scopus 로고
    • Two-dimensional crystallization of membrane proteins
    • Kühlbrandt, W. 1992. Two-dimensional crystallization of membrane proteins. Q. Rev. Biophys. 25:1-49.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 1-49
    • Kühlbrandt, W.1
  • 25
    • 0001666431 scopus 로고
    • X-ray monochromators
    • E. E. Koch, editor. North-Holland, Amsterdam
    • Matsushita, T., and H. Hashizume. 1983. X-ray monochromators. In Handbook on Synchrotron Radiation, Vol. 1A. E. E. Koch, editor. North-Holland, Amsterdam. 261-314.
    • (1983) Handbook on Synchrotron Radiation , vol.1 A , pp. 261-314
    • Matsushita, T.1    Hashizume, H.2
  • 27
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, and E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. Science. 277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 28
    • 0022766462 scopus 로고
    • The determination of label positions in membrane proteins by neutron and anomalous x-ray diffraction of powder samples
    • Plöhn, H.-J., and G. Büldt. 1986. The determination of label positions in membrane proteins by neutron and anomalous x-ray diffraction of powder samples. J. Appl. Crystalogr. 19:255-261.
    • (1986) J. Appl. Crystalogr. , vol.19 , pp. 255-261
    • Plöhn, H.-J.1    Büldt, G.2
  • 29
    • 0000123109 scopus 로고
    • Phase determination and Patterson maps from multiwavelength powder data
    • Prandl, W. 1990. Phase determination and Patterson maps from multiwavelength powder data. Acta Crystallogr. A. 46:988-992.
    • (1990) Acta Crystallogr. a , vol.46 , pp. 988-992
    • Prandl, W.1
  • 30
    • 0000105113 scopus 로고
    • Synchrotron radiation as a source for x-ray diffraction
    • Rosenbaum, G., K. C. Holmes, and J. Witz. 1971. Synchrotron radiation as a source for x-ray diffraction. Nature. 230:434-437.
    • (1971) Nature , vol.230 , pp. 434-437
    • Rosenbaum, G.1    Holmes, K.C.2    Witz, J.3
  • 31
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler, G. F. X., and P. A. Hargrave. 1995. Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA. 92: 11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 11578-11582
    • Schertler, G.F.X.1    Hargrave, P.A.2
  • 32
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G. F. X., C. Villa, and R. Henderson. 1993. Projection structure of rhodopsin. Nature. 362:770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 33
    • 0011075132 scopus 로고
    • A neutron diffraction study on the location of the polyene chain of retinal in bacteriorhodopsin
    • Seiff, F., I. Wallat, P. Ermann, and M. P. Heyn. 1985. A neutron diffraction study on the location of the polyene chain of retinal in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 82:3227-3231.
    • (1985) Proc. Natl. Acad. Sci. USA. , vol.82 , pp. 3227-3231
    • Seiff, F.1    Wallat, I.2    Ermann, P.3    Heyn, M.P.4
  • 35
    • 0342751336 scopus 로고
    • Anomalous x-ray scattering
    • M. Koch and E. Rubenstein, editors. Elsevier Science Publishers, Amsterdam
    • Stuhrmann, H. B., G. Goerigk, and B. Munk. 1991. Anomalous x-ray scattering. In Handbook on Synchrotron Radiation, Vol. 4. M. Koch and E. Rubenstein, editors. Elsevier Science Publishers, Amsterdam. 555-580.
    • (1991) Handbook on Synchrotron Radiation , vol.4 , pp. 555-580
    • Stuhrmann, H.B.1    Goerigk, G.2    Munk, B.3
  • 36
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein
    • Yang, W., W. A. Hendrickson, R. J. Crouch, and Y. Satow. 1990. Structure of ribonuclease H phased at 2 Å resolution by MAD analysis of the selenomethionyl protein. Science. 249:1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4


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