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Volumn 6, Issue SUPPL. 5, 2009, Pages

Large crystal growth by thermal control allows combined X-ray and neutron crystallographic studies to elucidate the protonation states in Aspergillus flavus urate oxidase

Author keywords

Crystal growth; H D exchange; Neutron and X ray crystallography; Phase diagram; Protonation states; Urate oxidase

Indexed keywords

CATALYSIS; CHEMOTHERAPY; CRYSTAL GROWTH; CRYSTALLIZATION; CYANIDES; DEUTERIUM; GRAIN BOUNDARIES; MINERALOGY; NEUTRONS; PHASE DIAGRAMS; PROTONATION; QUANTUM CHEMISTRY; SELF ASSEMBLY; SINGLE CRYSTALS; SUBSTRATES; X RAYS;

EID: 69949156416     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2009.0162.focus     Document Type: Conference Paper
Times cited : (19)

References (59)
  • 3
    • 0038892271 scopus 로고    scopus 로고
    • LSCALE-the new normalization, scaling and absorption correction program in the Daresbury Laue software suite
    • doi:10.1107/S0021889898015350
    • Arzt, S., Campbell, J. W., Harding, M. M., Hao, Q. & Helliwell, J. R. 1999 LSCALE-the new normalization, scaling and absorption correction program in the Daresbury Laue software suite. J. Appl. Cryst. 32, 554-562. (doi:10.1107/S0021889898015350)
    • (1999) J. Appl. Cryst. , vol.32 , pp. 554-562
    • Arzt, S.1    Campbell, J.W.2    Harding, M.M.3    Hao, Q.4    Helliwell, J.R.5
  • 4
    • 2142797534 scopus 로고    scopus 로고
    • Neutron diffraction studies on rubredoxin from Pyrococcus furiosus
    • DOI 10.1107/S0909049503024178
    • Bau, R. 2004 Neutron diffraction studies on rubredoxin from Pyrococcus furiosus. J. Synchrotron Radiat. 11, 76-79. (doi:10.1107/S0909049503024178) (Pubitemid 40085639)
    • (2004) Journal of Synchrotron Radiation , vol.11 , Issue.1 , pp. 76-79
    • Bau, R.1
  • 5
    • 0037391080 scopus 로고    scopus 로고
    • Seeds to crystals
    • doi:10.1016/S1047-8477(03)00039-X
    • Bergfors, T. 2003 Seeds to crystals. J. Struct. Biol. 142, 66-76. (doi:10.1016/S1047-8477(03)00039-X)
    • (2003) J. Struct. Biol. , vol.142 , pp. 66-76
    • Bergfors, T.1
  • 6
    • 0345158035 scopus 로고
    • Studies of completely deuteriated proteins
    • doi:10.1021/bi00906a033
    • Berns, D. S. 1963 Studies of completely deuteriated proteins. Biochemistry 6, 1377-1380. (doi:10.1021/bi00906a033)
    • (1963) Biochemistry , vol.6 , pp. 1377-1380
    • Berns, D.S.1
  • 7
    • 53449086885 scopus 로고    scopus 로고
    • Neutron crystallography: Opportunities, challenges, and limitations
    • doi:10.1016/j.sbi.2008.06.009
    • Blakeley, M., Langan, P., Niimura, N. & Podjarny, A. 2008 Neutron crystallography: opportunities, challenges, and limitations. Curr. Opin. Struct. Biol. 18, 593-600. (doi:10.1016/j.sbi.2008.06.009)
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 593-600
    • Blakeley, M.1    Langan, P.2    Niimura, N.3    Podjarny, A.4
  • 8
    • 0024036940 scopus 로고
    • Crystallization mechanisms in solution
    • doi:10.1016/0022-0248(88)90294-1
    • Boistelle, R. & Astier, P. 1988 Crystallization mechanisms in solution. J. Cryst. Growth 90, 14-30. (doi:10.1016/0022-0248(88)90294-1)
    • (1988) J. Cryst. Growth , vol.90 , pp. 14-30
    • Boistelle, R.1    Astier, P.2
  • 9
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase 'adapt' to solvent conditions
    • doi:10.1006/jmbi.1994.1741
    • Bonneté, F., Madern, D. & Zaccaï, G. 1994 Stability against denaturation mechanisms in halophilic malate dehydrogenase 'adapt' to solvent conditions. J. Mol. Biol. 244, 436-447. (doi:10.1006/jmbi.1994.1741)
    • (1994) J. Mol. Biol. , vol.244 , pp. 436-447
    • Bonneté, F.1    Madern, D.2    Zaccaï, G.3
  • 11
    • 0001541359 scopus 로고    scopus 로고
    • Comparison of solubility and interactions of aprotinin (BPTI) solutions in H2O and D2O
    • doi:10.1016/S0022-0248(00)00495-4
    • Budayova-Spano, M., Lafont, S., Astier, J. P., Ebel, C. & Veesler, S. 2000 Comparison of solubility and interactions of aprotinin (BPTI) solutions in H2O and D2O. J. Cryst. Growth 217, 311-319. (doi:10.1016/S0022-0248(00)00495-4)
    • (2000) J. Cryst. Growth , vol.217 , pp. 311-319
    • Budayova-Spano, M.1    Lafont, S.2    Astier, J.P.3    Ebel, C.4    Veesler, S.5
  • 12
    • 33645744389 scopus 로고    scopus 로고
    • A preliminary neutron diffraction study of rasburicase, a recombinant urate oxidase enzyme, complexed with 8-azaxanthin
    • doi:10.1107/S1744309106006439
    • Budayova-Spano, M., Bonneté, F., Ferté, N., El Hajji, M., Meilleur, F., Blakeley, M. P. & Castro, B. 2006 A preliminary neutron diffraction study of rasburicase, a recombinant urate oxidase enzyme, complexed with 8-azaxanthin. Acta Cryst. F 62, 306-309. (doi:10.1107/S1744309106006439)
    • (2006) Acta Cryst. F , vol.62 , pp. 306-309
    • Budayova-Spano, M.1    Bonneté, F.2    Ferté, N.3    El Hajji, M.4    Meilleur, F.5    Blakeley, M.P.6    Castro, B.7
  • 13
    • 33947321557 scopus 로고    scopus 로고
    • A methodology and an instrument for the temperature-controlled optimization of crystal growth
    • doi:10.1107/S0907444906054230
    • Budayova-Spano, M., Dauvergne, F., Audiffren, M., Bactivelane, T. & Cusack, S. 2007 A methodology and an instrument for the temperature-controlled optimization of crystal growth. Acta Cryst. D 63, 339-347. (doi:10.1107/ S0907444906054230)
    • (2007) Acta Cryst. D , vol.63 , pp. 339-347
    • Budayova-Spano, M.1    Dauvergne, F.2    Audiffren, M.3    Bactivelane, T.4    Cusack, S.5
  • 15
    • 0032138631 scopus 로고    scopus 로고
    • Temperature- dependent solubility of selected proteins
    • doi:10.1016/S0022-0248(98)00355-8
    • Christopher, G. K., Phipps, A. G. & Gray, R. J. 1998 Temperature- dependent solubility of selected proteins. J. Cryst. Growth 191, 820-826. (doi:10.1016/S0022-0248(98)00355-8)
    • (1998) J. Cryst. Growth , vol.191 , pp. 820-826
    • Christopher, G.K.1    Phipps, A.G.2    Gray, R.J.3
  • 16
    • 0035818441 scopus 로고    scopus 로고
    • A neutron laue diffraction study of endothiapepsin: Implications for the aspartic proteinase mechanism
    • DOI 10.1021/bi010626h
    • Coates, L., Erskine, P. T., Wood, S. P., Myles, D. A. & Cooper, J. B. 2001 A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism. Biochemistry 40, 149-157. (doi:10.1021/bi010626h) (Pubitemid 33043529)
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13149-13157
    • Coates, L.1    Erskine, P.T.2    Wood, S.P.3    Myles, D.A.A.4    Cooper, J.B.5
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 doi:10.1107/ S0907444994003112
    • Collaborative Computational Project, Number 4 1994 The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763. (doi:10.1107/S0907444994003112)
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 19
    • 33846041165 scopus 로고    scopus 로고
    • Protein crystallography under xenon and nitrous oxide pressure: Comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action
    • doi:10.1529/biophysj.106.093807
    • Colloc'h, N., Sopkova-de Oliveira Santos, J., Retailleau, P., Langlois d'Estainto, B., Gallois, B., Brisson, A., Risso, J. J., Lemaire, M. & Abraini, J. H. 2007 Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action. Biophys. J. 92, 217-224. (doi:10.1529/biophysj.106.093807)
    • (2007) Biophys. J. , vol.92 , pp. 217-224
    • Colloc'H, N.1    Sopkova-de Oliveira Santos, J.2    Retailleau, P.3    Langlois D'Estainto, B.4    Gallois, B.5    Brisson, A.6    Risso, J.J.7    Lemaire, M.8    Abraini, J.H.9
  • 20
    • 0033106268 scopus 로고    scopus 로고
    • Remarks about protein structure precision
    • doi:10.1107/S0907444998012645
    • Cruickshank, D. W. J. 1999 Remarks about protein structure precision. Acta Cryst. D 55, 583-601. (doi:10.1107/S0907444998012645)
    • (1999) Acta Cryst. D , vol.55 , pp. 583-601
    • Cruickshank, D.W.J.1
  • 21
    • 33751163048 scopus 로고    scopus 로고
    • The structure of concanavalin a and its bound solvent determined with small-molecule accuracy at 0.94 angstrom resolution
    • doi:10.1039/a704140c
    • Deacon, A., Gleichmann, T., Kalb, A. J., Price, H., Raftery, J., Bradbrook, G., Yariv, J. & Helliwell, J. R. 1997 The structure of concanavalin A and its bound solvent determined with small-molecule accuracy at 0.94 angstrom resolution. J. Chem. Soc. Faraday Trans. 93, 4305-4312. (doi:10.1039/a704140c)
    • (1997) J. Chem. Soc. Faraday Trans. , vol.93 , pp. 4305-4312
    • Deacon, A.1    Gleichmann, T.2    Kalb, A.J.3    Price, H.4    Raftery, J.5    Bradbrook, G.6    Yariv, J.7    Helliwell, J.R.8
  • 22
    • 0027109238 scopus 로고
    • Factors affecting the morphology of isocitrate lyase crystals
    • doi:10.1016/0022-0248(92)90238-E
    • De Mattei, R. C., Feigelson, R. S. & Weber, P. C. 1992 Factors affecting the morphology of isocitrate lyase crystals. J. Cryst. Growth 122, 152-160. (doi:10.1016/0022-0248(92)90238-E)
    • (1992) J. Cryst. Growth , vol.122 , pp. 152-160
    • De Mattei, R.C.1    Feigelson, R.S.2    Weber, P.C.3
  • 25
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • doi:10.1107/S0108767391001071
    • Engh, R. A. & Huber, R. 1991 Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400. (doi:10.1107/S0108767391001071)
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 27
    • 33645225169 scopus 로고    scopus 로고
    • Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase
    • doi:10.1016/j.febslet.2006.03.007
    • Gabison, L., Chiadmi, M., Colloc'h, N., Castro, B., El Hajji, M. & Prangé, T. 2006 Recapture of [S]-allantoin, the product of the two-step degradation of uric acid, by urate oxidase. FEBS Lett. 580, 2087-2091. (doi:10.1016/j.febslet.2006.03.007)
    • (2006) FEBS Lett. , vol.580 , pp. 2087-2091
    • Gabison, L.1    Chiadmi, M.2    Colloc'H, N.3    Castro, B.4    El Hajji, M.5    Prangé, T.6
  • 28
    • 48349128546 scopus 로고    scopus 로고
    • Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: Mechanistic implications
    • doi:10.1186/1472-6807-8-32
    • Gabison, L., Prangé, T., Colloc'h, N., El Hajji, M., Castro, B. & Chiadmi, M. 2008 Structural analysis of urate oxidase in complex with its natural substrate inhibited by cyanide: mechanistic implications. BMC Struct. Biol. 8, 32-40. (doi:10.1186/1472-6807-8-32)
    • (2008) BMC Struct. Biol. , vol.8 , pp. 32-40
    • Gabison, L.1    Prangé, T.2    Colloc'h, N.3    El Hajji, M.4    Castro, B.5    Chiadmi, M.6
  • 29
    • 0028173324 scopus 로고
    • The production and X-ray structure determination of perdeuterated Staphylococcal nuclease
    • doi:10.1016/0301-4622(94)00072-7
    • Gamble, T. R., Clauser, K. R. & Kossiakoff, A. A. 1994 The production and X-ray structure determination of perdeuterated Staphylococcal nuclease. Biophys. Chem. 53, 15-26. (doi:10.1016/0301-4622(94)00072-7)
    • (1994) Biophys. Chem. , vol.53 , pp. 15-26
    • Gamble, T.R.1    Clauser, K.R.2    Kossiakoff, A.A.3
  • 32
    • 3543083781 scopus 로고    scopus 로고
    • A preliminary time-of-flight neutron diffraction study of Streptomyces rubiginosus D-xylose isomerase
    • doi:10.1107/S0907444903025873
    • Hanson, B. L., Langan, P., Katz, A. K., Li, X., Harp, J. M., Glusker, J. P., Schoenborn, B. P. & Bunick, G. J. 2004 A preliminary time-of-flight neutron diffraction study of Streptomyces rubiginosus D-xylose isomerase. Acta Cryst. D 60, 241-249. (doi:10.1107/S0907444903025873)
    • (2004) Acta Cryst. D , vol.60 , pp. 241-249
    • Hanson, B.L.1    Langan, P.2    Katz, A.K.3    Li, X.4    Harp, J.M.5    Glusker, J.P.6    Schoenborn, B.P.7    Bunick, G.J.8
  • 34
    • 31344463247 scopus 로고    scopus 로고
    • Plasmodium falciparum glutathione S-transferase - Structural and mechanistic studies on ligand binding and enzyme inhibition
    • DOI 10.1110/ps.051891106
    • Hiller, N., Fritz-Wolf, K., Deponte, M., Wende, W., Zimmermann, H. & Becker, K. 2006 Plasmodium falciparum glutathione S-transferase-structural and mechanistic studies on ligand binding and enzyme inhibition. Protein Sci. 15, 281-289. (doi:10.1110/ps.051891106) (Pubitemid 43145000)
    • (2006) Protein Science , vol.15 , Issue.2 , pp. 281-289
    • Hiller, N.1    Fritz-Wolf, K.2    Deponte, M.3    Wende, W.4    Zimmermann, H.5    Becker, K.6
  • 35
    • 2542571016 scopus 로고    scopus 로고
    • Ultrahigh resolution drug design I: Details of interactions in human aldose reductase-inhibitor complex at 0.66 Å
    • doi:10.1002/prot.20015
    • Howard, E. I. et al. 2004 Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 Å. Proteins 55, 792-804. (doi:10.1002/prot.20015)
    • (2004) Proteins , vol.55 , pp. 792-804
    • Howard, E.I.1
  • 36
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • doi:10.1107/S0021889893005588
    • Kabsch, W. 1993 Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800. (doi:10.1107/S0021889893005588)
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 37
    • 0013796956 scopus 로고
    • The effect of D2O on the thermal stability of proteins. Thermodynamic parameters for the transfer of model compounds from H2O to D2O
    • doi:10.1021/j100893a054
    • Kresheck, G. C., Schneider, H. & Scheraga, H. A. 1965 The effect of D2O on the thermal stability of proteins. Thermodynamic parameters for the transfer of model compounds from H2O to D2O. J. Phys. Chem. 69, 3132-3144. (doi:10.1021/j100893a054)
    • (1965) J. Phys. Chem. , vol.69 , pp. 3132-3144
    • Kresheck, G.C.1    Schneider, H.2    Scheraga, H.A.3
  • 38
    • 34548354866 scopus 로고    scopus 로고
    • The effect of deuteration on protein structure: A high-resolution comparison of hydrogenous and perdeuterated haloalkane dehalogenase
    • DOI 10.1107/S0907444907037705, PII S0907444907037705
    • Liu, X., Hanson, B. L., Langan, P. & Viola, R. E. 2007 The effect of deuteration on protein structure: a high-resolution comparison of hydrogenous and perdeuterated haloalkane dehalogenase. Acta Cryst. D 63, 1000-1008. (doi:10.1107/S0907444907037705) (Pubitemid 47346826)
    • (2007) Acta Crystallographica Section D: Biological Crystallography , vol.63 , Issue.9 , pp. 1000-1008
    • Liu, X.1    Hanson, B.L.2    Langan, P.3    Viola, R.E.4
  • 39
    • 0027109237 scopus 로고
    • Versatile reactor for temperature controlled crystallization of biological macromolecules
    • DOI 10.1016/0022-0248(92)90240-J
    • Lorber, B. & Giegé, R. 1992 A versatile reactor for temperature controlled crystallization of biological macromolecules. J. Cryst. Growth 122, 168-175. (doi:10.1016/0022-0248(92)90240-J) (Pubitemid 23577825)
    • (1992) Journal of Crystal Growth , vol.122 , Issue.1-4 , pp. 168-175
    • Lorber, B.1    Giege, R.2
  • 40
    • 0028483512 scopus 로고
    • A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging- And sitting-drop vapor-diffusion and microdialysis experiments
    • doi:10.1107/S0021889893012713
    • Luft, J. R., Arakali, S. V., Kirisits, M. J., Kalenik, J., Wawrzak, I., Cody, V., Pangborn, W. A. & DeTitta, G. T. 1994 A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging- and sitting-drop vapor-diffusion and microdialysis experiments. J. Appl. Cryst. 27, 443-452. (doi:10.1107/S0021889893012713)
    • (1994) J. Appl. Cryst. , vol.27 , pp. 443-452
    • Luft, J.R.1    Arakali, S.V.2    Kirisits, M.J.3    Kalenik, J.4    Wawrzak, I.5    Cody, V.6    Pangborn, W.A.7    Detitta, G.T.8
  • 41
    • 0001062635 scopus 로고
    • Kinetics of carboxypeptidase action. I. Effect of various extrinsic factors on kinetic parameters
    • doi:10.1021/ja01153a090
    • Lumry, R., Smith, E. L. & Glantz, R. R. 1951 Kinetics of carboxypeptidase action. I. Effect of various extrinsic factors on kinetic parameters. J. Am. Chem. Soc. 73, 4330-4340. (doi:10.1021/ja01153a090)
    • (1951) J. Am. Chem. Soc. , vol.73 , pp. 4330-4340
    • Lumry, R.1    Smith, E.L.2    Glantz, R.R.3
  • 42
    • 2142692238 scopus 로고    scopus 로고
    • Crystallization of a large single crystal of cubic insulin for neutron protein crystallography
    • DOI 10.1107/S0909049503023859
    • Maeda, M., Chatake, T., Tanaka, I., Ostermann, A. & Niimura, N. 2004 Crystallization of a large single crystal of cubic insulin for neutron protein crystallography. J. Synchrotron Radiat. 11, 41-44. (doi:10.1107/ S0909049503023859) (Pubitemid 40085630)
    • (2004) Journal of Synchrotron Radiation , vol.11 , Issue.1 , pp. 41-44
    • Maeda, M.1    Chatake, T.2    Tanaka, I.3    Ostermann, A.4    Niimura, N.5
  • 43
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • doi:10.1016/0022-2836(68)90205-2
    • Matthews, B. W. 1968 Solvent content of protein crystals. J. Mol. Biol. 33, 491-497. (doi:10.1016/0022-2836(68)90205-2)
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 44
    • 0015987251 scopus 로고
    • Determination of molecular weight from protein crystals
    • doi:10.1016/0022-2836(74)90245-9
    • Matthews, B. W. 1974 Determination of molecular weight from protein crystals. J. Mol. Biol. 82, 513-526. (doi:10.1016/0022-2836(74)90245-9)
    • (1974) J. Mol. Biol. , vol.82 , pp. 513-526
    • Matthews, B.W.1
  • 45
    • 0033816837 scopus 로고    scopus 로고
    • Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies
    • DOI 10.1023/A:1008313530207
    • Morgan, W. D., Kragt, A. & Feeney, J. 2000 Expression of deuterium-isotope-labelled protein in the yeast Pichia pastoris for NMR studies. J. Biomol. NMR 17, 337-347. (doi:10.1023/A:1008313530207) (Pubitemid 30694290)
    • (2000) Journal of Biomolecular NMR , vol.17 , Issue.4 , pp. 337-347
    • Morgan, W.D.1    Kragt, A.2    Feeney, J.3
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • doi:10.1107/S0907444996012255
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. 1997 Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53, 240-255. (doi:10.1107/S0907444996012255)
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 47
    • 33749080560 scopus 로고    scopus 로고
    • Neutron protein crystallography: Current status and a brighter future
    • doi:10.1016/j.sbi.2006.08.010
    • Myles, D. A. A. 2006 Neutron protein crystallography: current status and a brighter future. Curr. Opin. Struct. Biol. 16, 630-637. (doi:10.1016/j.sbi. 2006.08.010)
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 630-637
    • Myles, D.A.A.1
  • 48
    • 0030565904 scopus 로고    scopus 로고
    • The crystallization of biological macromolecules from precipitates: Evidence for Ostwald ripening
    • PII S0022024896003624
    • Ng, J. D., Lorber, B., Witz, J., Theobald-Dietrich, A., Kern, D. & Giegé, R. 1996 The crystallization of biological macromolecules from precipitates: evidence for Ostwald ripening. J. Cryst. Growth 168, 50-62. (doi:10.1016/0022-0248(96)00362-4) (Pubitemid 126361801)
    • (1996) Journal of Crystal Growth , vol.168 , Issue.1-4 , pp. 50-62
    • Ng, J.D.1    Lorber, B.2    Witz, J.3    Theobald-Dietrich, A.4    Kern, D.5    Giege, R.6
  • 49
    • 37549049041 scopus 로고    scopus 로고
    • Neutron protein crystallography: Beyond the folding structure of biological macromolecules
    • doi:10.1107/S0108767307043498
    • Niimura, N. & Bau, R. 2008 Neutron protein crystallography: beyond the folding structure of biological macromolecules. Acta Cryst. A 64, 12-22. (doi:10.1107/S0108767307043498)
    • (2008) Acta Cryst. A , vol.64 , pp. 12-22
    • Niimura, N.1    Bau, R.2
  • 52
    • 7444239015 scopus 로고    scopus 로고
    • Complexed and ligand-free high resolution structures of urate oxidase (Uox) from Aspergillus flavus: A reassignment of the active site binding mode
    • doi:10.1107/S0907444903029718
    • Retailleau, P., Colloc'h, N., Vivarès, D., Bonneté, F., Castro, B., El Hajji, M., Mornon, J. P., Monard, G. & Prangé, T. 2004 Complexed and ligand-free high resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active site binding mode. Acta Cryst. D 60, 453-462. (doi:10.1107/S0907444903029718)
    • (2004) Acta Cryst. D , vol.60 , pp. 453-462
    • Retailleau, P.1    Colloc'H, N.2    Vivarès, D.3    Bonneté, F.4    Castro, B.5    El Hajji, M.6    Mornon, J.P.7    Monard, G.8    Prangé, T.9
  • 53
    • 24044454073 scopus 로고    scopus 로고
    • Urate oxidase from Aspergillus flavus: New crystal packing contacts in relation to the content of the active site
    • doi:10.1107/S0907444904031531
    • Retailleau, P., Colloc'h, N., Vivarès, D., Bonneté, F., Castro, B., El Hajji, M. & Prangé, T. 2005 Urate oxidase from Aspergillus flavus: new crystal packing contacts in relation to the content of the active site. Acta Cryst. D 61, 218-229. (doi:10.1107/S0907444904031531)
    • (2005) Acta Cryst. D , vol.61 , pp. 218-229
    • Retailleau, P.1    Colloc'h, N.2    Vivarès, D.3    Bonneté, F.4    Castro, B.5    El Hajji, M.6    Prangé, T.7
  • 54
    • 0034635974 scopus 로고    scopus 로고
    • Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin
    • doi:10.1073/pnas.060024697
    • Shu, F., Ramakrishnan, V. & Schoenborn, B. P. 2000 Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin. Proc. Natl Acad. Sci. USA 97, 3872-3877. (doi:10.1073/pnas.060024697)
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3872-3877
    • Shu, F.1    Ramakrishnan, V.2    Schoenborn, B.P.3
  • 55
    • 33947309173 scopus 로고    scopus 로고
    • La cristallisation des molécules Conséquences en termes de polymorphisme et faciès appliquées au domaine pharmaceutique Concepts de base
    • Veesler, S., Puel, F. & Fevotte, G. 2003 La cristallisation des molécules Conséquences en termes de polymorphisme et faciès appliquées au domaine pharmaceutique Concepts de base. STP Pharma Prat. 13, 1-32.
    • (2003) STP Pharma Prat. , vol.13 , pp. 1-32
    • Veesler, S.1    Puel, F.2    Fevotte, G.3
  • 58
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • doi:10.1016/S0969-2126(99)80086-0
    • Zhu, X. T., Kim, J. L., Newcomb, J. R., Rose, P. E., Stover, D. R., Toledo, L. M., Zhao, H. L. & Morgenstern, K. A. 1999 Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure 7, 651-661. (doi:10.1016/S0969-2126(99) 80086-0)
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.T.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6    Zhao, H.L.7    Morgenstern, K.A.8


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