메뉴 건너뛰기




Volumn 19, Issue 2, 2012, Pages 238-245

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; NITRIC OXIDE; NITRIC OXIDE REDUCTASE; NITROGEN OXIDE;

EID: 84856734126     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2213     Document Type: Article
Times cited : (102)

References (60)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification?
    • Zumft, W.G. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61, 533-616 (1997). (Pubitemid 28006959)
    • (1997) Microbiology and Molecular Biology Reviews , vol.61 , Issue.4 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 10444275550 scopus 로고    scopus 로고
    • Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type
    • DOI 10.1016/j.jinorgbio.2004.09.024, PII S0162013404002909, Heme-Diatomic Interactions, Part 1
    • Zumft, W.G. Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type. J. Inorg. Biochem. 99, 194-215 (2005). (Pubitemid 39642979)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 194-215
    • Zumft, W.G.1
  • 5
    • 19744380767 scopus 로고    scopus 로고
    • Nitric oxide detoxification systems enhance survival of Neisseria meningitidis in human macrophages and in nasopharyngeal mucosa
    • DOI 10.1128/IAI.73.6.3322-3329.2005
    • Stevanin, T.M., Moir, J.W. & Read, R.C. Nitric oxide detoxification systems enhance survival of Neisseria meningitidis in human macrophages and in nasopharyngeal mucosa. Infect. Immun. 73, 3322-3329 (2005). (Pubitemid 40745873)
    • (2005) Infection and Immunity , vol.73 , Issue.6 , pp. 3322-3329
    • Stevanin, T.M.1    Moir, J.W.B.2    Read, R.C.3
  • 6
    • 18044384871 scopus 로고    scopus 로고
    • Denitrification in pathogenic bacteria: For better or worst?
    • DOI 10.1016/j.tim.2005.03.001
    • Philippot, L. Denitrification in pathogenic bacteria: for better or worst? Trends Microbiol. 13, 191-192 (2005). (Pubitemid 40603898)
    • (2005) Trends in Microbiology , vol.13 , Issue.5 , pp. 191-192
    • Philippot, L.1
  • 7
    • 70349694213 scopus 로고    scopus 로고
    • Nitrous oxide (N2O): The dominant ozone-depleting substance emitted in the 21st century
    • Ravishankara, A.R., Daniel, J.S. & Portmann, R.W. Nitrous oxide (N2O): the dominant ozone-depleting substance emitted in the 21st century. Science 326, 123-125 (2009).
    • (2009) Science , vol.326 , pp. 123-125
    • Ravishankara, A.R.1    Daniel, J.S.2    Portmann, R.W.3
  • 8
    • 77957744758 scopus 로고    scopus 로고
    • The evolution and future of Earth's nitrogen cycle
    • Canfield, D.E., Glazer, A.N. & Falkowski, P.G. The evolution and future of Earth's nitrogen cycle. Science 330, 192-196 (2010).
    • (2010) Science , vol.330 , pp. 192-196
    • Canfield, D.E.1    Glazer, A.N.2    Falkowski, P.G.3
  • 9
    • 78149384651 scopus 로고    scopus 로고
    • Coupling of nitrous oxide and methane by global atmospheric chemistry
    • Prather, M.J. & Hsu, J. Coupling of nitrous oxide and methane by global atmospheric chemistry. Science 330, 952-954 (2010).
    • (2010) Science , vol.330 , pp. 952-954
    • Prather, M.J.1    Hsu, J.2
  • 10
    • 70349687228 scopus 로고    scopus 로고
    • Atmosphere. Nitrous oxide: No laughing matter
    • Wuebbles, D.J. Atmosphere. Nitrous oxide: no laughing matter. Science 326, 56-57 (2009).
    • (2009) Science , vol.326 , pp. 56-57
    • Wuebbles, D.J.1
  • 11
    • 11244302439 scopus 로고    scopus 로고
    • NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: Characterization of reaction intermediates that appear in the single turnover cycle
    • DOI 10.1074/jbc.M409996200
    • Kumita, H. et al. NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle. J. Biol. Chem. 279, 55247-55254 (2004). (Pubitemid 40066521)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55247-55254
    • Kumita, H.1    Matsuura, K.2    Hino, T.3    Takahashi, S.4    Hori, H.5    Fukumori, Y.6    Morishima, I.7    Shiro, Y.8
  • 12
    • 34249789578 scopus 로고    scopus 로고
    • Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins
    • DOI 10.1039/b604194a
    • Moënne-Loccoz, P. Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins. Nat. Prod. Rep. 24, 610-620 (2007). (Pubitemid 46848713)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 610-620
    • Moenne-Loccoz, P.1
  • 13
    • 72949111166 scopus 로고    scopus 로고
    • Rational design of a structural and functional nitric oxide reductase
    • Yeung, N. et al. Rational design of a structural and functional nitric oxide reductase. Nature 462, 1079-1082 (2009).
    • (2009) Nature , vol.462 , pp. 1079-1082
    • Yeung, N.1
  • 14
    • 33745203021 scopus 로고    scopus 로고
    • Reduction of nitric oxide in bacterial nitric oxide reductase-a theoretical model study
    • Blomberg, L.M., Blomberg, M.R. & Siegbahn, P.E. Reduction of nitric oxide in bacterial nitric oxide reductase-a theoretical model study. Biochim. Biophys. Acta 1757, 240-252 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 240-252
    • Blomberg, L.M.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 15
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • DOI 10.1016/0014-5793(94)80228-9
    • Saraste, M. & Castresana, J. Cytochrome oxidase evolved by tinkering with denitrification enzymes. FEBS Lett. 341, 1-4 (1994). (Pubitemid 24089178)
    • (1994) FEBS Letters , vol.341 , Issue.1 , pp. 1-4
    • Saraste, M.1
  • 16
    • 0029988772 scopus 로고    scopus 로고
    • Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512
    • Fujiwara, T. & Fukumori, Y. Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512. J. Bacteriol. 178, 1866-1871 (1996). (Pubitemid 26110528)
    • (1996) Journal of Bacteriology , vol.178 , Issue.7 , pp. 1866-1871
    • Fujiwara, T.1    Fukumori, Y.2
  • 18
    • 58149503700 scopus 로고    scopus 로고
    • Vectorial proton transfer coupled to reduction of O2 and NO by a heme-copper oxidase
    • Huang, Y., Reimann, J., Lepp, H., Drici, N. & Adelroth, P. Vectorial proton transfer coupled to reduction of O2 and NO by a heme-copper oxidase. Proc. Natl. Acad. Sci. USA 105, 20257-20262 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20257-20262
    • Huang, Y.1    Reimann, J.2    Lepp, H.3    Drici, N.4    Adelroth, P.5
  • 19
    • 61449231809 scopus 로고    scopus 로고
    • Accommodation of two diatomic molecules in cytochrome bo: Insights into NO reductase activity in terminal oxidases
    • Hayashi, T. et al. Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases. Biochemistry 48, 883-890 (2009).
    • (2009) Biochemistry , vol.48 , pp. 883-890
    • Hayashi, T.1
  • 20
    • 0037133132 scopus 로고    scopus 로고
    • Proton and electron pathways in the bacterial nitric oxide reductase
    • DOI 10.1021/bi0121050
    • Hendriks, J.H., Jasaitis, A., Saraste, M. & Verkhovsky, M.I. Proton and electron pathways in the bacterial nitric oxide reductase. Biochemistry 41, 2331-2340 (2002). (Pubitemid 34160895)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2331-2340
    • Hendriks, J.H.M.1    Jasaitis, A.2    Saraste, M.3    Verkhovsky, M.I.4
  • 21
    • 34247472629 scopus 로고    scopus 로고
    • A pathway for protons in nitric oxide reductase from Paracoccus denitrificans
    • DOI 10.1016/j.bbabio.2007.03.006, PII S0005272807000680
    • Reimann, J., Flock, U., Lepp, H., Honigmann, A. & Adelroth, P. A pathway for protons in nitric oxide reductase from Paracoccus denitrificans. Biochim. Biophys. Acta 1767, 362-373 (2007). (Pubitemid 46659879)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.5 , pp. 362-373
    • Reimann, J.1    Flock, U.2    Lepp, H.3    Honigmann, A.4    Adelroth, P.5
  • 22
    • 78650307247 scopus 로고    scopus 로고
    • Structural basis of biological N2O generation by bacterial nitric oxide reductase
    • Hino, T. et al. Structural basis of biological N2O generation by bacterial nitric oxide reductase. Science 330, 1666-1670 (2010).
    • (2010) Science , vol.330 , pp. 1666-1670
    • Hino, T.1
  • 23
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & Michel, H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376, 660-669 (1995).
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 24
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å
    • Tsukihara, T. et al. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272, 1136-1144 (1996).
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1
  • 26
    • 77954809358 scopus 로고    scopus 로고
    • The structure of cbb3 cytochrome oxidase provides insights into proton pumping
    • Buschmann, S. et al. The structure of cbb3 cytochrome oxidase provides insights into proton pumping. Science 329, 327-330 (2010).
    • (2010) Science , vol.329 , pp. 327-330
    • Buschmann, S.1
  • 27
    • 32544438038 scopus 로고    scopus 로고
    • Proton transfer in bacterial nitric oxide reductase
    • DOI 10.1042/BST0340188
    • Flock, U., Reimann, J. & Adelroth, P. Proton transfer in bacterial nitric oxide reductase. Biochem. Soc. Trans. 34, 188-190 (2006). (Pubitemid 43235568)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.1 , pp. 188-190
    • Flock, U.1    Reimann, J.2    Adelroth, P.3
  • 28
    • 42949093313 scopus 로고    scopus 로고
    • Defining the proton entry point in the bacterial respiratory nitric-oxide reductase
    • Flock, U. et al. Defining the proton entry point in the bacterial respiratory nitric-oxide reductase. J. Biol. Chem. 283, 3839-3845 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 3839-3845
    • Flock, U.1
  • 29
    • 0032836317 scopus 로고    scopus 로고
    • Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16
    • DOI 10.1016/S0014-5793(99)01315-0, PII S0014579399013150
    • Cramm, R., Pohlmann, A. & Friedrich, B. Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. FEBS Lett. 460, 6-10 (1999). (Pubitemid 29479234)
    • (1999) FEBS Letters , vol.460 , Issue.1 , pp. 6-10
    • Cramm, R.1    Pohlmann, A.2    Friedrich, B.3
  • 30
    • 0141704413 scopus 로고    scopus 로고
    • 2:NO oxidoreductase from the hyperthermophilic archaeon Pyrobaculum aerophilum
    • DOI 10.1074/jbc.M300857200
    • de Vries, S., Strampraad, M.J., Lu, S., Moenne-Loccoz, P. & Schroder, I. Purification and characterization of the MQH2:NO oxidoreductase from the hyperthermophilic archaeon Pyrobaculum aerophilum. J. Biol. Chem. 278, 35861-35868 (2003). (Pubitemid 37139903)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 35861-35868
    • De Vries, S.1    Strampraad, M.J.F.2    Lu, S.3    Moenne-Loccoz, P.4    Schroder, I.5
  • 31
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana, J., Lubben, M., Saraste, M. & Higgins, D.G. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J. 13, 2516-2525 (1994). (Pubitemid 24188384)
    • (1994) EMBO Journal , vol.13 , Issue.11 , pp. 2516-2525
    • Castresana, J.1    Lubben, M.2    Saraste, M.3    Higgins, D.G.4
  • 32
    • 0026675309 scopus 로고
    • Restoration of a lost metal-binding site: Construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex
    • van der Oost, J. et al. Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex. EMBO J. 11, 3209-3217 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3209-3217
    • Van Der Oost, J.1
  • 33
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • DOI 10.1016/S0005-2728(01)00169-4, PII S0005272801001694
    • Pereira, M.M., Santana, M. & Teixeira, M. A novel scenario for the evolution of haem-copper oxygen reductases. Biochim. Biophys. Acta 1505, 185-208 (2001). (Pubitemid 32378771)
    • (2001) Biochimica et Biophysica Acta - Bioenergetics , vol.1505 , Issue.2-3 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 34
    • 0025732606 scopus 로고
    • Acid denatured apo-cytochrome c is a random coil: Evidence from small-angle X-ray scattering and dynamic light scattering
    • Damaschun, G., Damaschun, H., Gast, K., Gernat, C. & Zirwer, D. Acid denatured apo-cytochrome c is a random coil: evidence from small-angle X-ray scattering and dynamic light scattering. Biochim. Biophys. Acta 1078, 289-295 (1991).
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 289-295
    • Damaschun, G.1    Damaschun, H.2    Gast, K.3    Gernat, C.4    Zirwer, D.5
  • 35
    • 0035190144 scopus 로고    scopus 로고
    • Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme
    • DOI 10.1128/JB.183.1.189-199.2001
    • Butland, G., Spiro, S., Watmough, N.J. & Richardson, D.J. Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme. J. Bacteriol. 183, 189-199 (2001). (Pubitemid 32003123)
    • (2001) Journal of Bacteriology , vol.183 , Issue.1 , pp. 189-199
    • Butland, G.1    Spiro, S.2    Watmough, N.J.3    Richardson, D.J.4
  • 36
    • 33846270025 scopus 로고    scopus 로고
    • A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme
    • DOI 10.1042/BJ20060856
    • Thorndycroft, F.H., Butland, G., Richardson, D.J. & Watmough, N.J. A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme. Biochem. J. 401, 111-119 (2007). (Pubitemid 46114605)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 111-119
    • Thorndycrof, F.H.1    Butland, G.2    Richardson, D.J.3    Watmough, N.J.4
  • 37
    • 77952700938 scopus 로고    scopus 로고
    • Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
    • Lin, Y.W. et al. Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin. Proc. Natl. Acad. Sci. USA 107, 8581-8586 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8581-8586
    • Lin, Y.W.1
  • 38
    • 1942423697 scopus 로고    scopus 로고
    • Dynamic Water Networks in Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Molecular Dynamics Simulations
    • Olkhova, E., Hutter, M.C., Lill, M.A., Helms, V. & Michel, H. Dynamic water networks in cytochrome c oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations. Biophys. J. 86, 1873-1889 (2004). (Pubitemid 38524385)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 1873-1889
    • Olkhova, E.1    Hutter, M.C.2    Lill, M.A.3    Helms, V.4    Michel, H.5
  • 39
    • 47049112847 scopus 로고    scopus 로고
    • Quinol oxidation by c-type cytochromes: Structural characterization of the menaquinol binding site of NrfHA
    • Rodrigues, M.L., Scott, K.A., Sansom, M.S., Pereira, I.A. & Archer, M. Quinol oxidation by c-type cytochromes: structural characterization of the menaquinol binding site of NrfHA. J. Mol. Biol. 381, 341-350 (2008).
    • (2008) J. Mol. Biol. , vol.381 , pp. 341-350
    • Rodrigues, M.L.1    Scott, K.A.2    Sansom, M.S.3    Pereira, I.A.4    Archer, M.5
  • 40
    • 0033788953 scopus 로고    scopus 로고
    • The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site
    • Abramson, J. et al. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. 7, 910-917 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 910-917
    • Abramson, J.1
  • 41
    • 0034649368 scopus 로고    scopus 로고
    • Electrogenic reactions of cytochrome bd
    • Jasaitis, A. et al. Electrogenic reactions of cytochrome bd. Biochemistry 39, 13800-13809 (2000).
    • (2000) Biochemistry , vol.39 , pp. 13800-13809
    • Jasaitis, A.1
  • 43
    • 33747351535 scopus 로고    scopus 로고
    • Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes
    • Paraskevopoulos, K., Antonyuk, S.V., Sawers, R.G., Eady, R.R. & Hasnain, S.S. Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes. J. Mol. Biol. 362, 55-65 (2006).
    • (2006) J. Mol. Biol. , vol.362 , pp. 55-65
    • Paraskevopoulos, K.1    Antonyuk, S.V.2    Sawers, R.G.3    Eady, R.R.4    Hasnain, S.S.5
  • 44
    • 58149305974 scopus 로고    scopus 로고
    • Was nitric oxide the first deep electron sink?
    • Ducluzeau, A.L. et al. Was nitric oxide the first deep electron sink? Trends Biochem. Sci. 34, 9-15 (2009).
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 9-15
    • Ducluzeau, A.L.1
  • 45
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • DOI 10.1093/nar/gkg581
    • Kawabata, T. MATRAS: A program for protein 3D structure comparison. Nucleic Acids Res. 31, 3367-3369 (2003). (Pubitemid 37442161)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3367-3369
    • Kawabata, T.1
  • 46
    • 34548479264 scopus 로고    scopus 로고
    • 3 oxidase) of heme-copper oxygen reductases
    • DOI 10.1021/bi700659y
    • Hemp, J. et al. Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases. Biochemistry 46, 9963-9972 (2007). (Pubitemid 47378586)
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 9963-9972
    • Hemp, J.1    Han, H.2    Jung, H.R.3    Kaplan, S.4    Martinez, T.J.5    Gennis, R.B.6
  • 47
    • 77950258771 scopus 로고    scopus 로고
    • Nitrite-driven anaerobic methane oxidation by oxygenic bacteria
    • Ettwig, K.F. et al. Nitrite-driven anaerobic methane oxidation by oxygenic bacteria. Nature 464, 543-548 (2010).
    • (2010) Nature , vol.464 , pp. 543-548
    • Ettwig, K.F.1
  • 48
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: A new tool to explore routes from protein clefts, pockets and cavities
    • Petrek, M. et al. CAVER: a new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinformatics 7, 316 (2006).
    • (2006) BMC Bioinformatics , vol.7 , pp. 316
    • Petrek, M.1
  • 49
    • 0020004138 scopus 로고
    • 551 from Pseudomonas aeruginosa refined at 1.6 À resolution and comparison of the two redox forms
    • DOI 10.1016/0022-2836(82)90335-7
    • Matsuura, Y., Takano, T. & Dickerson, R.E. Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156, 389-409 (1982). (Pubitemid 12116318)
    • (1982) Journal of Molecular Biology , vol.156 , Issue.2 , pp. 389-409
    • Matsuura, Y.1    Takano, T.2    Dickerson, R.E.3
  • 50
    • 56249143434 scopus 로고    scopus 로고
    • A novel type of monoheme cytochrome c: Biochemical and structural characterization at 1.23 Å resolution of Rhodothermus marinus cytochrome c
    • Stelter, M. et al. A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 Å resolution of Rhodothermus marinus cytochrome c. Biochemistry 47, 11953-11963 (2008).
    • (2008) Biochemistry , vol.47 , pp. 11953-11963
    • Stelter, M.1
  • 51
    • 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. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997). (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 52
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • DOI 10.1107/S0907444903017694
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M. & Paciorek, W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D Biol. Crystallogr. 59, 2023-2030 (2003). (Pubitemid 37399336)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.11 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 53
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P. & Leslie, A.G. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D Biol. Crystallogr. 52, 30-42 (1996).
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 55
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. Version 1.2 of the crystallography and NMR system. Nat. Protoc. 2, 2728-2733 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 59
    • 48749148224 scopus 로고
    • Rattle: A "velocity" version of the shake algorithm for molecular dynamics calculations
    • Andersen, H.C. Rattle: A "velocity" version of the shake algorithm for molecular dynamics calculations. J. Comput. Phys. 52, 24-34 (1983).
    • (1983) J. Comput. Phys. , vol.52 , pp. 24-34
    • Andersen, H.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.