메뉴 건너뛰기




Volumn 425, Issue 17, 2013, Pages 3121-3136

Cysteine dioxygenase structures from pH 4 to 9: Consistent Cys-persulfenate formation at intermediate pH and a Cys-bound enzyme at higher pH

Author keywords

high spin ferrous iron; iron sulfur; metalloenzyme; sulfur metabolism; thiol oxidation

Indexed keywords

CYSTEINE DIOXYGENASE; IRON;

EID: 84881663551     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.05.028     Document Type: Article
Times cited : (61)

References (55)
  • 2
    • 0028564882 scopus 로고
    • The activities of rat hepatic cysteine dioxygenase and cysteinesulfinate decarboxylase are regulated in a reciprocal manner in response to dietary casein level
    • P.J. Bagley, and M.H. Stipanuk The activities of rat hepatic cysteine dioxygenase and cysteinesulfinate decarboxylase are regulated in a reciprocal manner in response to dietary casein level J. Nutr. 124 1994 2410 2421
    • (1994) J. Nutr. , vol.124 , pp. 2410-2421
    • Bagley, P.J.1    Stipanuk, M.H.2
  • 3
    • 34547127140 scopus 로고    scopus 로고
    • Overexpression of cysteine dioxygenase reduces intracellular cysteine and glutathione pools in HepG2/C3A cells
    • J.E. Dominy Jr, J. Hwang, and M.H. Stipanuk Overexpression of cysteine dioxygenase reduces intracellular cysteine and glutathione pools in HepG2/C3A cells Am. J. Physiol. Endocrinol. Metab. 293 2007 E62 E69
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.293
    • Dominy, Jr.J.E.1    Hwang, J.2    Stipanuk, M.H.3
  • 4
    • 45549085195 scopus 로고    scopus 로고
    • Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity
    • J.E. Dominy Jr, J. Hwang, S. Guo, L.L. Hirschberger, S. Zhang, and M.H. Stipanuk Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity J. Biol. Chem. 283 2008 12188 12201
    • (2008) J. Biol. Chem. , vol.283 , pp. 12188-12201
    • Dominy, Jr.J.E.1    Hwang, J.2    Guo, S.3    Hirschberger, L.L.4    Zhang, S.5    Stipanuk, M.H.6
  • 5
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism: Pathways for production and removal of homocysteine and cysteine
    • M.H. Stipanuk Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine Annu. Rev. Nutr. 24 2004 539 577
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 6
    • 80053225374 scopus 로고    scopus 로고
    • Knockout of the murine cysteine dioxygenase gene results in severe impairment in ability to synthesize taurine and an increased catabolism of cysteine to hydrogen sulfide
    • I. Ueki, H.B. Roman, A. Valli, K. Fieselmann, J. Lam, and R. Peters Knockout of the murine cysteine dioxygenase gene results in severe impairment in ability to synthesize taurine and an increased catabolism of cysteine to hydrogen sulfide Am. J. Physiol. Endocrinol. Metab. 301 2011 E668 E684
    • (2011) Am. J. Physiol. Endocrinol. Metab. , vol.301
    • Ueki, I.1    Roman, H.B.2    Valli, A.3    Fieselmann, K.4    Lam, J.5    Peters, R.6
  • 7
    • 0025165272 scopus 로고
    • Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson's and Alzheimer's disease
    • M.T. Heafield, S. Fearn, G.B. Steventon, R.H. Waring, A.C. Williams, and S.G. Sturman Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson's and Alzheimer's disease Neurosci. Lett. 110 1990 216 220
    • (1990) Neurosci. Lett. , vol.110 , pp. 216-220
    • Heafield, M.T.1    Fearn, S.2    Steventon, G.B.3    Waring, R.H.4    Williams, A.C.5    Sturman, S.G.6
  • 8
    • 0028094409 scopus 로고
    • Sulfate metabolism is abnormal in patients with rheumatoid arthritis. Confirmation by in vivo biochemical findings
    • H. Bradley, A. Gough, R.S. Sokhi, A. Hassell, R. Waring, and P. Emery Sulfate metabolism is abnormal in patients with rheumatoid arthritis. Confirmation by in vivo biochemical findings J. Rheumatol. 21 1994 1192 1196
    • (1994) J. Rheumatol. , vol.21 , pp. 1192-1196
    • Bradley, H.1    Gough, A.2    Sokhi, R.S.3    Hassell, A.4    Waring, R.5    Emery, P.6
  • 9
    • 84866952731 scopus 로고    scopus 로고
    • Cysteine dioxygenase 1 is a tumor suppressor gene silenced by promoter methylation in multiple human cancers
    • M. Brait, S. Ling, J.K. Nagpal, X. Chang, H.L. Park, and J. Lee Cysteine dioxygenase 1 is a tumor suppressor gene silenced by promoter methylation in multiple human cancers PLoS One 7 2012 e44951
    • (2012) PLoS One , vol.7 , pp. 44951
    • Brait, M.1    Ling, S.2    Nagpal, J.K.3    Chang, X.4    Park, H.L.5    Lee, J.6
  • 10
    • 33745854127 scopus 로고    scopus 로고
    • Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation
    • C.R. Simmons, Q. Liu, Q. Huang, Q. Hao, T.P. Begley, P.A. Karplus, and M.H. Stipanuk Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation J. Biol. Chem. 281 2006 18723 18733
    • (2006) J. Biol. Chem. , vol.281 , pp. 18723-18733
    • Simmons, C.R.1    Liu, Q.2    Huang, Q.3    Hao, Q.4    Begley, T.P.5    Karplus, P.A.6    Stipanuk, M.H.7
  • 12
  • 13
    • 33746622949 scopus 로고    scopus 로고
    • Identification and characterization of bacterial cysteine dioxygenases: A new route of cysteine degradation for eubacteria
    • J.E. Dominy Jr., C.R. Simmons, P.A. Karplus, A.M. Gehring, and M.H. Stipanuk Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria J. Bacteriol. 188 2006 5561 5569
    • (2006) J. Bacteriol. , vol.188 , pp. 5561-5569
    • Dominy, Jr.J.E.1    Simmons, C.R.2    Karplus, P.A.3    Gehring, A.M.4    Stipanuk, M.H.5
  • 14
    • 81755177462 scopus 로고    scopus 로고
    • Correlating crosslink formation with enzymatic activity in cysteine dioxygenase
    • E. Siakkou, M.T. Rutledge, S.M. Wilbanks, and G.N. Jameson Correlating crosslink formation with enzymatic activity in cysteine dioxygenase Biochim. Biophys. Acta 1814 2011 2003 2009
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 2003-2009
    • Siakkou, E.1    Rutledge, M.T.2    Wilbanks, S.M.3    Jameson, G.N.4
  • 15
    • 84860496752 scopus 로고    scopus 로고
    • Addition of an external electron donor to in vitro assays of cysteine dioxygenase precludes the need for exogenous iron
    • E.M. Imsand, C.W. Njeri, and H.R. Ellis Addition of an external electron donor to in vitro assays of cysteine dioxygenase precludes the need for exogenous iron Arch. Biochem. Biophys. 521 2012 10 17
    • (2012) Arch. Biochem. Biophys. , vol.521 , pp. 10-17
    • Imsand, E.M.1    Njeri, C.W.2    Ellis, H.R.3
  • 16
    • 34047273745 scopus 로고    scopus 로고
    • An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor
    • S. Ye, X. Wu, L. Wei, D. Tang, P. Sun, M. Bartlam, and Z. Rao An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor J. Biol. Chem. 282 2007 3391 3402
    • (2007) J. Biol. Chem. , vol.282 , pp. 3391-3402
    • Ye, S.1    Wu, X.2    Wei, L.3    Tang, D.4    Sun, P.5    Bartlam, M.6    Rao, Z.7
  • 18
    • 77954829588 scopus 로고    scopus 로고
    • Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: Nature of the ferrous and ferric cysteine adducts and mechanistic implications
    • J.D. Gardner, B.S. Pierce, B.G. Fox, and T.C. Brunold Spectroscopic and computational characterization of substrate-bound mouse cysteine dioxygenase: nature of the ferrous and ferric cysteine adducts and mechanistic implications Biochemistry 49 2010 6033 6041
    • (2010) Biochemistry , vol.49 , pp. 6033-6041
    • Gardner, J.D.1    Pierce, B.S.2    Fox, B.G.3    Brunold, T.C.4
  • 19
    • 79952761655 scopus 로고    scopus 로고
    • Theoretical study on the mechanism of the oxygen activation process in cysteine dioxygenase enzymes
    • D. Kumar, W. Thiel, and S.P. de Visser Theoretical study on the mechanism of the oxygen activation process in cysteine dioxygenase enzymes J. Am. Chem. Soc. 133 2011 3869 3882
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3869-3882
    • Kumar, D.1    Thiel, W.2    De Visser, S.P.3
  • 20
    • 34547136935 scopus 로고    scopus 로고
    • Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: Electronic structure of the active site and mechanistic implications
    • B.S. Pierce, J.D. Gardner, L.J. Bailey, T.C. Brunold, and B.G. Fox Characterization of the nitrosyl adduct of substrate-bound mouse cysteine dioxygenase by electron paramagnetic resonance: electronic structure of the active site and mechanistic implications Biochemistry 46 2007 8569 8578
    • (2007) Biochemistry , vol.46 , pp. 8569-8578
    • Pierce, B.S.1    Gardner, J.D.2    Bailey, L.J.3    Brunold, T.C.4    Fox, B.G.5
  • 21
    • 81855172118 scopus 로고    scopus 로고
    • Single turnover of substrate-bound ferric cysteine dioxygenase with superoxide anion: Enzymatic reactivation, product formation, and a transient intermediate
    • J.A. Crawford, W. Li, and B.S. Pierce Single turnover of substrate-bound ferric cysteine dioxygenase with superoxide anion: enzymatic reactivation, product formation, and a transient intermediate Biochemistry 50 2011 10241 10253
    • (2011) Biochemistry , vol.50 , pp. 10241-10253
    • Crawford, J.A.1    Li, W.2    Pierce, B.S.3
  • 22
    • 36849079937 scopus 로고    scopus 로고
    • The mechanism of cysteine oxygenation by cysteine dioxygenase enzymes
    • S. Aluri, and S.P. de Visser The mechanism of cysteine oxygenation by cysteine dioxygenase enzymes J. Am. Chem. Soc. 129 2007 14846 14847
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14846-14847
    • Aluri, S.1    De Visser, S.P.2
  • 23
    • 63849098305 scopus 로고    scopus 로고
    • Why do cysteine dioxygenase enzymes contain a 3-His ligand motif rather than a 2His/1Asp motif like most nonheme dioxygenases?
    • S.P. de Visser, and G.D. Straganz Why do cysteine dioxygenase enzymes contain a 3-His ligand motif rather than a 2His/1Asp motif like most nonheme dioxygenases? J. Phys. Chem. A 113 2009 1835 1846
    • (2009) J. Phys. Chem. A , vol.113 , pp. 1835-1846
    • De Visser, S.P.1    Straganz, G.D.2
  • 25
    • 0035196519 scopus 로고    scopus 로고
    • Persulfoxide: Key intermediate in reactions of singlet oxygen with sulfides
    • E.L. Clennan Persulfoxide: key intermediate in reactions of singlet oxygen with sulfides Acc. Chem. Res. 34 2001 875 884
    • (2001) Acc. Chem. Res. , vol.34 , pp. 875-884
    • Clennan, E.L.1
  • 26
    • 0000865869 scopus 로고    scopus 로고
    • Oxygen capture by sulfur in nickel thiolates
    • C.A. Grapperhaus, and M.Y. Darensbourg Oxygen capture by sulfur in nickel thiolates Acc. Chem. Res. 31 1998 451 459
    • (1998) Acc. Chem. Res. , vol.31 , pp. 451-459
    • Grapperhaus, C.A.1    Darensbourg, M.Y.2
  • 27
    • 0001117776 scopus 로고
    • Divergent pathways for the addition of dioxygen to sulfur in nickel cis-dithiolates - An isotopomeric analysis
    • P.J. Farmer, T. Solouki, T. Soma, D.H. Russell, and M.Y. Darensbourg Divergent pathways for the addition of dioxygen to sulfur in nickel cis-dithiolates - an isotopomeric analysis Inorg. Chem. 32 1993 4171 4173
    • (1993) Inorg. Chem. , vol.32 , pp. 4171-4173
    • Farmer, P.J.1    Solouki, T.2    Soma, T.3    Russell, D.H.4    Darensbourg, M.Y.5
  • 28
    • 84855841546 scopus 로고    scopus 로고
    • Mechanism of S-oxygenation by a cysteine dioxygenase model complex
    • D. Kumar, G.N. Sastry, D.P. Goldberg, and S.P. de Visser Mechanism of S-oxygenation by a cysteine dioxygenase model complex J. Phys. Chem. A 116 2012 582 591
    • (2012) J. Phys. Chem. A , vol.116 , pp. 582-591
    • Kumar, D.1    Sastry, G.N.2    Goldberg, D.P.3    De Visser, S.P.4
  • 29
    • 84861617333 scopus 로고    scopus 로고
    • Addition of dioxygen to an N4S(thiolate) iron(II) cysteine dioxygenase model gives a structurally characterized sulfinato-iron(II) complex
    • A.C. McQuilken, Y. Jiang, M.A. Siegler, and D.P. Goldberg Addition of dioxygen to an N4S(thiolate) iron(II) cysteine dioxygenase model gives a structurally characterized sulfinato-iron(II) complex J. Am. Chem. Soc. 134 2012 8758 8761
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8758-8761
    • McQuilken, A.C.1    Jiang, Y.2    Siegler, M.A.3    Goldberg, D.P.4
  • 30
    • 84865693355 scopus 로고    scopus 로고
    • Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes
    • A.C. McQuilken, and D.P. Goldberg Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes Dalton Trans. 41 2012 10883 10899
    • (2012) Dalton Trans. , vol.41 , pp. 10883-10899
    • McQuilken, A.C.1    Goldberg, D.P.2
  • 31
    • 15444380484 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase
    • S.C. Chai, A.A. Jerkins, J.J. Banik, I. Shalev, J.L. Pinkham, P.C. Uden, and M.J. Maroney Heterologous expression, purification, and characterization of recombinant rat cysteine dioxygenase J. Biol. Chem. 280 2005 9865 9869
    • (2005) J. Biol. Chem. , vol.280 , pp. 9865-9869
    • Chai, S.C.1    Jerkins, A.A.2    Banik, J.J.3    Shalev, I.4    Pinkham, J.L.5    Uden, P.C.6    Maroney, M.J.7
  • 32
    • 33646087886 scopus 로고    scopus 로고
    • Expression, purification, and kinetic characterization of recombinant rat cysteine dioxygenase, a non-heme metalloenzyme necessary for regulation of cellular cysteine levels
    • C.R. Simmons, L.L. Hirschberger, M.S. Machi, and M.H. Stipanuk Expression, purification, and kinetic characterization of recombinant rat cysteine dioxygenase, a non-heme metalloenzyme necessary for regulation of cellular cysteine levels Protein Expr. Purif. 47 2006 74 81
    • (2006) Protein Expr. Purif. , vol.47 , pp. 74-81
    • Simmons, C.R.1    Hirschberger, L.L.2    MacHi, M.S.3    Stipanuk, M.H.4
  • 33
    • 33744935293 scopus 로고    scopus 로고
    • Probes of the catalytic site of cysteine dioxygenase
    • S.C. Chai, J.R. Bruyere, and M.J. Maroney Probes of the catalytic site of cysteine dioxygenase J. Biol. Chem. 281 2006 15774 15779
    • (2006) J. Biol. Chem. , vol.281 , pp. 15774-15779
    • Chai, S.C.1    Bruyere, J.R.2    Maroney, M.J.3
  • 34
    • 77955093007 scopus 로고    scopus 로고
    • Simplified cysteine dioxygenase activity assay allows simultaneous quantitation of both substrate and product
    • E. Siakkou, S.M. Wilbanks, and G.N. Jameson Simplified cysteine dioxygenase activity assay allows simultaneous quantitation of both substrate and product Anal. Biochem. 405 2010 127 131
    • (2010) Anal. Biochem. , vol.405 , pp. 127-131
    • Siakkou, E.1    Wilbanks, S.M.2    Jameson, G.N.3
  • 35
    • 84856868395 scopus 로고    scopus 로고
    • A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase
    • E.P. Tchesnokov, S.M. Wilbanks, and G.N. Jameson A strongly bound high-spin iron(II) coordinates cysteine and homocysteine in cysteine dioxygenase Biochemistry 51 2012 257 264
    • (2012) Biochemistry , vol.51 , pp. 257-264
    • Tchesnokov, E.P.1    Wilbanks, S.M.2    Jameson, G.N.3
  • 38
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 39
    • 48849104435 scopus 로고    scopus 로고
    • Data mining of metal ion environments present in protein structures
    • H. Zheng, M. Chruszcz, P. Lasota, L. Lebioda, and W. Minor Data mining of metal ion environments present in protein structures J. Inorg. Biochem. 102 2008 1765 1776
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 1765-1776
    • Zheng, H.1    Chruszcz, M.2    Lasota, P.3    Lebioda, L.4    Minor, W.5
  • 40
    • 34447643050 scopus 로고    scopus 로고
    • 2 in aqueous solution - Basic principles and a simple heuristic description
    • 2 in aqueous solution - basic principles and a simple heuristic description Chemosphere 68 2007 2080 2084
    • (2007) Chemosphere , vol.68 , pp. 2080-2084
    • Morgan, B.1    Lahav, O.2
  • 41
    • 33244476516 scopus 로고    scopus 로고
    • Application of Badger's rule to heme and non-heme iron-oxygen bonds: An examination of ferryl protonation states
    • M.T. Green Application of Badger's rule to heme and non-heme iron-oxygen bonds: an examination of ferryl protonation states J. Am. Chem. Soc. 128 2006 1902 1906
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1902-1906
    • Green, M.T.1
  • 42
    • 0036850996 scopus 로고    scopus 로고
    • Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation
    • M. Weik, J. Berges, M.L. Raves, P. Gros, S. McSweeney, and I. Silman Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation J. Synchrotron Radiat. 9 2002 342 346
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 342-346
    • Weik, M.1    Berges, J.2    Raves, M.L.3    Gros, P.4    McSweeney, S.5    Silman, I.6
  • 43
    • 70349840614 scopus 로고    scopus 로고
    • Structural changes common to catalysis in the Tpx peroxiredoxin subfamily
    • A. Hall, B. Sankaran, L.B. Poole, and P.A. Karplus Structural changes common to catalysis in the Tpx peroxiredoxin subfamily J. Mol. Biol. 393 2009 867 881
    • (2009) J. Mol. Biol. , vol.393 , pp. 867-881
    • Hall, A.1    Sankaran, B.2    Poole, L.B.3    Karplus, P.A.4
  • 45
    • 1842687872 scopus 로고    scopus 로고
    • Biomolecular cryocrystallography: Structural changes during flash-cooling
    • B. Halle Biomolecular cryocrystallography: structural changes during flash-cooling Proc. Natl Acad. Sci. USA 101 2004 4793 4798
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4793-4798
    • Halle, B.1
  • 46
    • 0038143254 scopus 로고    scopus 로고
    • The anomalous pKa of Tyr-9 in glutathione S-transferase A1-1 catalyzes product release
    • C.A. Ibarra, P. Chowdhury, J.W. Petrich, and W.M. Atkins The anomalous pKa of Tyr-9 in glutathione S-transferase A1-1 catalyzes product release J. Biol. Chem. 278 2003 19257 19265
    • (2003) J. Biol. Chem. , vol.278 , pp. 19257-19265
    • Ibarra, C.A.1    Chowdhury, P.2    Petrich, J.W.3    Atkins, W.M.4
  • 47
    • 0032502245 scopus 로고    scopus 로고
    • Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases
    • B.P. Schlegel, J.M. Jez, and T.M. Penning Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases Biochemistry 37 1998 3538 3548
    • (1998) Biochemistry , vol.37 , pp. 3538-3548
    • Schlegel, B.P.1    Jez, J.M.2    Penning, T.M.3
  • 48
    • 33744475636 scopus 로고    scopus 로고
    • Preparation, crystallization and X-ray diffraction analysis to 1.5 Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation
    • C.R. Simmons, Q. Hao, and M.H. Stipanuk Preparation, crystallization and X-ray diffraction analysis to 1.5 Å resolution of rat cysteine dioxygenase, a mononuclear iron enzyme responsible for cysteine thiol oxidation Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 61 2005 1013 1016
    • (2005) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.61 , pp. 1013-1016
    • Simmons, C.R.1    Hao, Q.2    Stipanuk, M.H.3
  • 50
    • 0003027568 scopus 로고    scopus 로고
    • Recent advances in phasing
    • K.S. Wilson, G. Davies, A.W. Ashton, S. Bailey, Daresbury Laboratory Warrington, UK
    • P.R. Evans Recent advances in phasing K.S. Wilson, G. Davies, A.W. Ashton, S. Bailey, Proc. CCP4 Study Weekend 1997 Daresbury Laboratory Warrington, UK 97 102
    • (1997) Proc. CCP4 Study Weekend , pp. 97-102
    • Evans, P.R.1
  • 52
    • 70349597601 scopus 로고    scopus 로고
    • Electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • N.W. Moriarty, R.W. Grosse-Kunstleve, and P.D. Adams Electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation Acta Crystallogr., Sect. D: Biol. Crystallogr. 65 2009 1074 1080
    • (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 53
    • 0033613812 scopus 로고    scopus 로고
    • Visualizing and quantifying molecular goodness-of-fit: Small-probe contact dots with explicit hydrogen atoms
    • J.M. Word, S.C. Lovell, T.H. LaBean, H.C. Taylor, M.E. Zalis, and B.K. Presley Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms J. Mol. Biol. 285 1999 1711 1733
    • (1999) J. Mol. Biol. , vol.285 , pp. 1711-1733
    • Word, J.M.1    Lovell, S.C.2    Labean, T.H.3    Taylor, H.C.4    Zalis, M.E.5    Presley, B.K.6
  • 55
    • 84881669190 scopus 로고    scopus 로고
    • Simplified error estimation a la Cruickshank in macromolecular crystallography
    • G.N. Murshudov, and E.J. Dodson Simplified error estimation a la Cruickshank in macromolecular crystallography CCP4 Newsletter January 1997 1997 Diseases
    • (1997) CCP4 Newsletter January 1997
    • Murshudov, G.N.1    Dodson, E.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.