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Volumn 278, Issue 9, 2011, Pages 1506-1521

Probing the reactivity of different forms of azurin by flavin photoreduction

Author keywords

Cu protein; electron transfer; flash photolysis; flavin; protein cavity

Indexed keywords

AZURIN; COPPER; COPPER PROTEIN; GLYCINE; HISTIDINE; IMIDAZOLE; LIGAND; QUERCETIN; RIBOFLAVIN DERIVATIVE; WATER;

EID: 79955075757     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08067.x     Document Type: Article
Times cited : (8)

References (67)
  • 1
    • 0032956179 scopus 로고    scopus 로고
    • Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin
    • DOI 10.1007/s007750050294
    • Sokerina EV, Ullmann GM, van Pouderoyen G, Canters GW, &, Kostic NM, (1999) Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin. J Biol Inorg Chem 4, 111-121. (Pubitemid 29113818)
    • (1999) Journal of Biological Inorganic Chemistry , vol.4 , Issue.1 , pp. 111-121
    • Sokerina, E.V.1    Ullmann, G.M.2    Van Pouderoyen, G.3    Canters, G.W.4    Kostic, N.M.5
  • 3
    • 0343822781 scopus 로고
    • Photoinduced electron-transfer from zinc cytochrome-C to plastocyanin is gated by surface-diffusion within the metalloprotein complex
    • Zhou JS, &, Kostic NM, (1992) Photoinduced electron-transfer from zinc cytochrome-C to plastocyanin is gated by surface-diffusion within the metalloprotein complex. J Am Chem Soc 114 3562-3563.
    • (1992) J Am Chem Soc , vol.114 , pp. 3562-3563
    • Zhou, J.S.1    Kostic, N.M.2
  • 4
    • 0033963393 scopus 로고    scopus 로고
    • Construction of artificial photosynthetic reaction centers on a protein surface: Vectorial, multistep, and proton-coupled electron transfer for long- lived charge separation
    • DOI 10.1021/ja991406i
    • Hu YZ, Tsukiji S, Shinkai S, Oishi S, &, Hamachi I, (2000) Construction of artificial photosynthetic reaction centers on a protein surface: vectorial, multistep, and proton-coupled electron transfer for long-lived charge separation. J Am Chem Soc 122, 241-253. (Pubitemid 30061053)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.2 , pp. 241-253
    • Hu, Y.-Z.1    Tsukiji, S.2    Shinkai, S.3    Oishi, S.4    Hamachi, I.5
  • 5
    • 2942547311 scopus 로고    scopus 로고
    • Electron-transfer chemistry of Ru-linker-(heme)-modified myoglobin: Rapid intraprotein reduction of a photogenerated porphyrin cation radical
    • Immoos CE, Di Bilio AJ, Cohen MS, Van der Veer W, Gray HB, &, Farmer PJ, (2004) Electron-transfer chemistry of Ru-linker-(heme)-modified myoglobin: rapid intraprotein reduction of a photogenerated porphyrin cation radical. Inorg Chem 43, 3593-3596.
    • (2004) Inorg Chem , vol.43 , pp. 3593-3596
    • Immoos, C.E.1    Di Bilio, A.J.2    Cohen, M.S.3    Van Der Veer, W.4    Gray, H.B.5    Farmer, P.J.6
  • 8
    • 0023651177 scopus 로고
    • Influence of 8-alpha-imidazole substitution of the Fmn cofactor on the rate of electron-transfer from the neutral semiquinones of 2 flavodoxins to cytochrome-C
    • De Francesco R, Tollin G, &, Edmondson DE, (1987) Influence of 8-alpha-imidazole substitution of the Fmn cofactor on the rate of electron-transfer from the neutral semiquinones of 2 flavodoxins to cytochrome-C. Biochemistry 26, 5036-5042.
    • (1987) Biochemistry , vol.26 , pp. 5036-5042
    • De Francesco, R.1    Tollin, G.2    Edmondson, D.E.3
  • 9
    • 0032994640 scopus 로고    scopus 로고
    • Glucose oxidase electrodes via reconstitution of the apo-enzyme: Tailoring of novel glucose biosensors
    • DOI 10.1016/S0003-2670(98)00688-6, PII S0003267098006886
    • Katz E, Riklin A, Heleg-Shabtai V, Willner I, &, Buckmann AF, (1999) Glucose oxidase electrodes via reconstitution of the apo-enzyme: tailoring of novel glucose biosensors. Anal Chim Acta 385, 45-58. (Pubitemid 29131528)
    • (1999) Analytica Chimica Acta , vol.385 , Issue.1-3 , pp. 45-58
    • Katz, E.1    Riklin, A.2    Heleg-Shabtai, V.3    Willner, I.4    Buckmann, A.F.5
  • 10
    • 0025130573 scopus 로고
    • Structure and oxidation-reduction behavior of 1-deaza-FMN flavodoxins: Modulation of redox potentials in flavodoxins
    • Ludwig ML, Schopfer LM, Metzger AL, Pattridge KA, &, Massey V, (1990) Structure and oxidation reduction behavior of 1-deaza-fmn flavodoxins- modulation of redox potentials in flavodoxins. Biochemistry 29, 10364-10375. (Pubitemid 20384546)
    • (1990) Biochemistry , vol.29 , Issue.45 , pp. 10364-10375
    • Ludwig, M.L.1    Schopfer, L.M.2    Metzger, A.L.3    Pattridge, K.A.4    Massey, V.5
  • 11
    • 0037054860 scopus 로고    scopus 로고
    • Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: Spectral, photochemical and binding studies on the ferrous derivatives
    • DOI 10.1016/S0301-4622(02)00085-6, PII S0301462202000856
    • Silkstone G, Stanway G, Brzezinski P, &, Wilson MT, (2002) Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives. Biophys Chem 98, 65-77. (Pubitemid 34785982)
    • (2002) Biophysical Chemistry , vol.98 , Issue.1-2 , pp. 65-77
    • Silkstone, G.1    Stanway, G.2    Brzezinski, P.3    Wilson, M.T.4
  • 12
    • 0000726214 scopus 로고    scopus 로고
    • Design and semisynthesis of photoactive myoglobin bearing ruthenium tris(2,2â€2-bipyridine) using cofactor-reconstitution
    • Hamachi I, Tanaka S, Tsukiji S, Shinkai S, &, Oishi S, (1998) Design and semisynthesis of photoactive myoglobin bearing ruthenium tris(2,2â€2-bipyridine) using cofactor-reconstitution. Inorg Chem 37, 4380-4388. (Pubitemid 128483148)
    • (1998) Inorganic Chemistry , vol.37 , Issue.17 , pp. 4380-4388
    • Hamachi, I.1    Tanaka, S.2    Tsukiji, S.3    Shinkai, S.4    Oishi, S.5
  • 13
    • 33745343303 scopus 로고
    • Structural features of azurin at 2.7 A-resolution
    • Adman ET, &, Jensen LH, (1981) Structural features of azurin at 2.7 A-resolution. Isr J Chem 21, 8-12.
    • (1981) Isr J Chem , vol.21 , pp. 8-12
    • Adman, E.T.1    Jensen, L.H.2
  • 14
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0: A pH-induced conformational transition involves a peptide bond flip
    • Nar H, Messerschmidt A, Huber R, Vandekamp M, &, Canters GW, (1991) Crystal-structure analysis of oxidized Pseudomonas aeruginosa azurin at Ph 5.5 and Ph 9.0-A pH-induced conformational transition involves a peptide-bond flip. J Mol Biol 221, 765-772. (Pubitemid 121003417)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.3 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 15
    • 12044251595 scopus 로고
    • Creation of type-1 and type-2 copper sites by addition of exogenous ligands to the Pseudomonas aeruginosa azurin His117Gly mutant
    • den Blaauwen T, &, Canters GW, (1993) Creation of type-1 and type-2 copper sites by addition of exogenous ligands to the Pseudomonas aeruginosa azurin His117Gly mutant. J Am Chem Soc 115, 1121-1129.
    • (1993) J Am Chem Soc , vol.115 , pp. 1121-1129
    • Den Blaauwen, T.1    Canters, G.W.2
  • 16
    • 0000904136 scopus 로고    scopus 로고
    • Electron relaxation and solvent accessibility of the metal site in wild-type and mutated azurins as determined from nuclear magnetic relaxation dispersion experiments
    • Kroes SJ, Salgado J, Parigi G, Luchinat C, &, Canters GW, (1996) Electron relaxation and solvent accessibility of the metal site in wild-type and mutated azurins as determined from nuclear magnetic relaxation dispersion experiments. J Biol Inorg Chem 1, 551-559. (Pubitemid 126490067)
    • (1996) Journal of Biological Inorganic Chemistry , vol.1 , Issue.6 , pp. 551-559
    • Kroes, S.J.1    Salgado, J.2    Parigi, G.3    Luchinat, C.4    Canters, G.W.5
  • 17
    • 0034625312 scopus 로고    scopus 로고
    • The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin
    • Jeuken LJC, Ubbink M, Bitter JH, van Vliet P, Meyer-Klaucke W, &, Canters GW, (2000) The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin. J Mol Biol 299, 737-755.
    • (2000) J Mol Biol , vol.299 , pp. 737-755
    • Jeuken, L.J.C.1    Ubbink, M.2    Bitter, J.H.3    Van Vliet, P.4    Meyer-Klaucke, W.5    Canters, G.W.6
  • 18
    • 0027440118 scopus 로고
    • Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands
    • DOI 10.1021/bi00097a025
    • den Blaauwen T, Hoitink CWG, Canters GW, Han J, Loehr TM, &, Sandersloehr J, (1993) Resonance Raman-spectroscopy of the azurin His117Gly mutant-interconversion of type-1 and type-2 copper sites through exogenous ligands. Biochemistry 32, 12455-12464. (Pubitemid 23357968)
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12455-12464
    • Den Blaauwen, T.1    Hoitink, C.W.G.2    Canters, G.W.3    Han, J.4    Loehr, T.M.5    Sanders- Loehr, J.6
  • 21
    • 0034645617 scopus 로고    scopus 로고
    • Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: The electron-transfer and redox-coupled ligand binding properties of His117Gly azurin
    • DOI 10.1021/ja0006144
    • Jeuken LJC, van Vliet P, Verbeet MP, Camba R, Mcevoy JP, Armstrong FA, &, Canters GW, (2000) Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: the electron-transfer and redox-coupled ligand binding properties of His117Gly azurin. J Am Chem Soc 122, 12186-12194. (Pubitemid 32062256)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.49 , pp. 12186-12194
    • Jueken, L.J.C.1    Van Vliet, P.2    Verbeet, M.Ph.3    Camba, R.4    McEvoy, J.P.5    Armstrong, F.A.6    Canters, G.W.7
  • 22
    • 77958072064 scopus 로고    scopus 로고
    • Outer-sphere effects on reduction potentials of copper sites in proteins: The curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin
    • Lancaster KM, Sproules S, Palmer JH, Richards JH, &, Gray HB, (2010) Outer-sphere effects on reduction potentials of copper sites in proteins: the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin. J Am Chem Soc 132, 14590-14595.
    • (2010) J Am Chem Soc , vol.132 , pp. 14590-14595
    • Lancaster, K.M.1    Sproules, S.2    Palmer, J.H.3    Richards, J.H.4    Gray, H.B.5
  • 24
    • 0028820053 scopus 로고
    • Use of flavin photochemistry to probe intraprotein and interprotein electron-transfer mechanisms
    • Tollin G, (1995) Use of flavin photochemistry to probe intraprotein and interprotein electron-transfer mechanisms. J Bioenerg Biomembr 27, 303-309.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 303-309
    • Tollin, G.1
  • 25
    • 0017186397 scopus 로고
    • Nicotinamide-dependent one-electron and 2-electron (flavin) oxidoreduction - Thermodynamics, kinetics, and mechanism
    • Blankenhorn G, (1976) Nicotinamide-dependent one-electron and 2-electron (flavin) oxidoreduction-thermodynamics, kinetics, and mechanism. Eur J Biochem 67, 67-80.
    • (1976) Eur J Biochem , vol.67 , pp. 67-80
    • Blankenhorn, G.1
  • 26
    • 0022295394 scopus 로고
    • Effect of pH on oxidation-reduction potentials of 8α-N-imidazole- substituted flavins
    • Williamson G, &, Edmondson DE, (1985) Effect of Ph on oxidation-reduction potentials of 8-alpha-N-imidazole-substituted flavins. Biochemistry 24, 7790-7797. (Pubitemid 16140516)
    • (1985) Biochemistry , vol.24 , Issue.26 , pp. 7790-7797
    • Williamson, G.1    Edmondson, D.E.2
  • 27
    • 0014299673 scopus 로고
    • A potentiometric study of flavin semiquinone equilibrium
    • Draper RD, &, Ingraham LL, (1968) A potentiometric study of flavin semiquinone equilibrium. Arch Biochem Biophys 125, 802-808.
    • (1968) Arch Biochem Biophys , vol.125 , pp. 802-808
    • Draper, R.D.1    Ingraham, L.L.2
  • 29
    • 0015525675 scopus 로고
    • Studies on succinate dehydrogenase - 8alpha-histidyl-Fad as active center of succinate dehydrogenase
    • Walker WH, Singer TP, Hemmeric P, and, Ghisla S, (1972) Studies on succinate dehydrogenase-8alpha-histidyl-Fad as active center of succinate dehydrogenase. Eur J Biochem 26, 279-289.
    • (1972) Eur J Biochem , vol.26 , pp. 279-289
    • Walker, W.H.1    Singer, T.P.2    Hemmeric, P.3    Ghisla, S.4
  • 30
    • 0001849357 scopus 로고
    • Structure, synthesis and physical properties of covalently bound flavins and 6- and 8-hydroxyflavins
    • (Mueller F. ed) Boca Raton, FL, USA.
    • Edmondson DE, &, De Francesco R, (1991) Structure, synthesis and physical properties of covalently bound flavins and 6- and 8-hydroxyflavins. In Chemistry and Biochemistry of Flavoenzymes (, Mueller F, ed), pp 73-103. Boca Raton, FL, USA.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 73-103
    • Edmondson, D.E.1    De Francesco, R.2
  • 31
    • 0024042818 scopus 로고
    • Pka values of the 8-alpha-imidazole substituents in selected flavoenzymes containing 8-alpha-histidylflavins
    • De Francesco R, &, Edmondson DE, (1988) Pka values of the 8-alpha-imidazole substituents in selected flavoenzymes containing 8-alpha-histidylflavins. Arch Biochem Biophys 264, 281-287.
    • (1988) Arch Biochem Biophys , vol.264 , pp. 281-287
    • De Francesco, R.1    Edmondson, D.E.2
  • 32
    • 33947353272 scopus 로고
    • The theory of reversible two-step oxidation involving free radicals
    • Michaelis L, &, Schubert MP, (1938) The theory of reversible two-step oxidation involving free radicals. Chem Rev 22, 437-470.
    • (1938) Chem Rev , vol.22 , pp. 437-470
    • Michaelis, L.1    Schubert, M.P.2
  • 33
    • 0033570113 scopus 로고    scopus 로고
    • The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide. A reappraisal
    • DOI 10.1046/j.1432-1327.1999.00767.x
    • Mayhew SG, (1999) The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide-a reappraisal. Eur J Biochem 265, 698-702. (Pubitemid 29489003)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.2 , pp. 698-702
    • Mayhew, S.G.1
  • 34
    • 0027759256 scopus 로고
    • Use of laser flash photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron transfer mechanisms
    • DOI 10.1016/0301-4622(93)85014-9
    • Tollin G, Hurley JK, Hazzard JT, &, Meyer TE, (1993) Use of laser flash-photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron-transfer mechanisms. Biophys Chem 48, 259-279. (Pubitemid 24029734)
    • (1993) Biophysical Chemistry , vol.48 , Issue.2 , pp. 259-279
    • Tollin, G.1    Hurley, J.K.2    Hazzard, J.T.3    Meyer, T.E.4
  • 35
    • 0017855692 scopus 로고
    • Light-mediated reduction of flavoproteins with flavins as catalysts
    • Massey V, Stankovich M, &, Hemmerich P, (1978) Light-mediated reduction of flavoproteins with flavins as catalysts. Biochemistry 17, 1-8. (Pubitemid 8257940)
    • (1978) Biochemistry , vol.17 , Issue.1 , pp. 1-8
    • Massey, V.1    Stankovich, M.2    Hemmerich, P.3
  • 36
    • 0025765409 scopus 로고
    • Transient kinetics of flavin-photosensitized oxidation of reduced redox proteins - Comparison of C-type cytochromes and plastocyanins
    • Navarro JA, Delarosa MA, &, Tollin G, (1991) Transient kinetics of flavin-photosensitized oxidation of reduced redox proteins-comparison of C-type cytochromes and plastocyanins. Eur J Biochem 199, 239-243.
    • (1991) Eur J Biochem , vol.199 , pp. 239-243
    • Navarro, J.A.1    Delarosa, M.A.2    Tollin, G.3
  • 37
    • 0026763765 scopus 로고
    • Engineering protein-structure for electron-transfer function in photosynthetic reaction centers
    • Moser CC, &, Dutton PL, (1992) Engineering protein-structure for electron-transfer function in photosynthetic reaction centers. Biochim Biophys Acta 1101, 171-176.
    • (1992) Biochim Biophys Acta , vol.1101 , pp. 171-176
    • Moser, C.C.1    Dutton, P.L.2
  • 38
    • 0030070183 scopus 로고    scopus 로고
    • The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa
    • DOI 10.1016/0014-5793(96)00076-2
    • Gorren ACF, den Blaauwen T, Canters GW, Hopper DJ, &, Duine JA, (1996) The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa. FEBS Lett 381, 140-142. (Pubitemid 26070438)
    • (1996) FEBS Letters , vol.381 , Issue.1-2 , pp. 140-142
    • Gorren, A.C.F.1    Den Blaauwen, T.2    Canters, G.W.3    Hopper, D.J.4    Duine, J.A.5
  • 39
    • 0025282719 scopus 로고
    • Site-directed mutagenesis reveals that the hydrophobic patch of azurin mediates electron transfer
    • Vandekamp M, Floris R, Hali FC, &, Canters GW, (1990) Site-directed mutagenesis reveals that the hydrophobic patch of azurin mediates electron-transfer. J Am Chem Soc 112, 907-908. (Pubitemid 20093859)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.2 , pp. 907-908
    • Van De Kamp, M.1    Floris, R.2    Hali, F.C.3    Canters, G.W.4
  • 40
    • 0025252558 scopus 로고
    • Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome-C551 and nitrite reductase
    • Vandekamp M, Silvestrini MC, Brunori M, Vanbeeumen J, Hali FC, &, Canters GW, (1990) Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome-C551 and nitrite reductase. Eur J Biochem 194, 109-118.
    • (1990) Eur J Biochem , vol.194 , pp. 109-118
    • Vandekamp, M.1    Silvestrini, M.C.2    Brunori, M.3    Vanbeeumen, J.4    Hali, F.C.5    Canters, G.W.6
  • 41
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • DOI 10.1021/bi0260841
    • Diederix REM, Ubbink M, &, Canters GW, (2002) Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry 41, 13067-13077. (Pubitemid 35215792)
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 13067-13077
    • Diederix, R.E.M.1    Ubbink, M.2    Canters, G.W.3
  • 44
    • 0024990129 scopus 로고
    • Purification and characterization of a nonreconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa Azu gene in Escherichia coli
    • van de Kamp M, Hali FC, Rosato N, Agro AF, &, Canters GW, (1990) Purification and characterization of a nonreconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa Azu gene in Escherichia coli. Biochim Biophys Acta 1019, 283-292.
    • (1990) Biochim Biophys Acta , vol.1019 , pp. 283-292
    • Van De Kamp, M.1    Hali, F.C.2    Rosato, N.3    Agro, A.F.4    Canters, G.W.5
  • 46
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton PL, (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol 54, 411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 48
    • 0028956793 scopus 로고
    • Purification and physicochemical properties of the low-potential cytochrome C(549) from the cyanobacterium Synechocystis Sp Pcc-6803
    • Navarro JA, Hervas M, Delacerda B, &, Delarosa MA, (1995) Purification and physicochemical properties of the low-potential cytochrome C(549) from the cyanobacterium Synechocystis Sp Pcc-6803. Arch Biochem Biophys 318, 46-52.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 46-52
    • Navarro, J.A.1    Hervas, M.2    Delacerda, B.3    Delarosa, M.A.4
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr Pt A 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 49749140771 scopus 로고    scopus 로고
    • Pseudo-merohedral twinning in crystals of the dihaem c-type cytochrome DHC2 from Geobacter sulfurreducens
    • Heitmann D, &, Einsle O, (2008) Pseudo-merohedral twinning in crystals of the dihaem c-type cytochrome DHC2 from Geobacter sulfurreducens. Acta Crystallogr D Biol Crystallogr 64, 993-999.
    • (2008) Acta Crystallogr D Biol Crystallogr , vol.64 , pp. 993-999
    • Heitmann, D.1    Einsle, O.2
  • 51
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • DOI 10.1016/S0076-6879(97)76068-3
    • Yeates TO, (1997) Detecting and overcoming crystal twinning. Macromol Crystallogr Pt A 276, 344-358. (Pubitemid 27085613)
    • (1997) Methods in Enzymology , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 53
    • 0001037287 scopus 로고
    • On Order-Disorder Structures (OD-Structures)
    • Dornberger-Schiff K, (1956) On Order-Disorder Structures (OD-Structures). Acta Crystallogr A 9, 593-601.
    • (1956) Acta Crystallogr A , vol.9 , pp. 593-601
    • Dornberger-Schiff, K.1
  • 54
    • 24844451551 scopus 로고
    • Reliability index for centrosymmetric and non-centrosymmetric structures
    • Phillips DC, Rogers D, &, Wilson AJC, (1950) Reliability index for centrosymmetric and non-centrosymmetric structures. Acta Crystallogr A 3, 398-399.
    • (1950) Acta Crystallogr A , vol.3 , pp. 398-399
    • Phillips, D.C.1    Rogers, D.2    Wilson, A.J.C.3
  • 55
    • 2542518743 scopus 로고
    • Partial Fourier syntheses and their application to the solution of certain crystal structures
    • Buerger MJ, (1956) Partial Fourier syntheses and their application to the solution of certain crystal structures. Proc Natl Acad Sci USA 42, 776-781.
    • (1956) Proc Natl Acad Sci USA , vol.42 , pp. 776-781
    • Buerger, M.J.1
  • 56
    • 84944813717 scopus 로고
    • The influence of rational dependence on the probability-distribution of structure factors
    • Gramlich V, (1984) The influence of rational dependence on the probability-distribution of structure factors. Acta Crystallogr A 40, 610-616.
    • (1984) Acta Crystallogr A , vol.40 , pp. 610-616
    • Gramlich, V.1
  • 57
    • 84944811835 scopus 로고
    • Direct methods for structures with superstructure effects
    • Böhme R, (1982) Direct methods for structures with superstructure effects. Acta Crystallogr A 38, 318-326.
    • (1982) Acta Crystallogr A , vol.38 , pp. 318-326
    • Böhme, R.1
  • 58
    • 0006058486 scopus 로고
    • Direct methods and superstructures.1. Effects of the pseudotranslations on the reciprocal space
    • Cascarano G, Giacovazzo C, &, Luic M, (1985) Direct methods and superstructures.1. Effects of the pseudotranslations on the reciprocal space. Acta Crystallogr A 41, 544-551.
    • (1985) Acta Crystallogr A , vol.41 , pp. 544-551
    • Cascarano, G.1    Giacovazzo, C.2    Luic, M.3
  • 59
    • 0002575114 scopus 로고
    • Direct methods and structures showing superstructure effects.2. A probabilistic theory of triplet invariants
    • Cascarano G, Giacovazzo C, &, Luic M, (1987) Direct methods and structures showing superstructure effects.2. A probabilistic theory of triplet invariants. Acta Crystallogr A 43, 14-22.
    • (1987) Acta Crystallogr A , vol.43 , pp. 14-22
    • Cascarano, G.1    Giacovazzo, C.2    Luic, M.3
  • 61
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • DOI 10.1107/S0907444901012471
    • Read RJ, (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 57, 1373-1382. (Pubitemid 36117185)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.10 , pp. 1373-1382
    • Read, R.J.1
  • 66
    • 0000330205 scopus 로고    scopus 로고
    • On the use of the merging R factor as a quality indicator for X-ray data
    • Weiss MS, &, Hilgenfeld R, (1997) On the use of the merging R factor as a quality indicator for X-ray data. J Appl Crystallogr 30, 203-205. (Pubitemid 127477069)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.2 , pp. 203-205
    • Weiss, M.S.1    Hilgenfeld, R.2


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