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Volumn 305, Issue , 2005, Pages 155-165

X-Ray Crystallography of Protein-Ligand Interactions

Author keywords

Cocrystallization; concentration; cryocrystallography; crystallography; diffraction; diffusion; kinetic crystallography; monochromatic; reaction intermediate; soaking; trapping; triggering

Indexed keywords

ALLOSTERISM; CRYSTAL STRUCTURE; CRYSTALLIZATION; DATA INTERPRETATION; DIFFUSION; KINETICS; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION; ARTICLE; CHEMISTRY; IN VITRO STUDY; MACROMOLECULE; METABOLISM; METHODOLOGY; PROTEIN BINDING;

EID: 21344439774     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1385/1-59259-912-5:155     Document Type: Chapter
Times cited : (7)

References (60)
  • 3
    • 0033857394 scopus 로고    scopus 로고
    • Crystallographic structure determination of unstable species
    • Schlichting, I. (2000) Crystallographic structure determination of unstable species. Acc. Chem Res. 33, 532–538.
    • (2000) Acc. Chem Res , vol.33 , pp. 532-538
    • Schlichting, I.1
  • 4
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: ligand binding to myoglobin
    • Schlichting, I. and Chu, K. (2000) Trapping intermediates in the crystal: ligand binding to myoglobin. Curr. Opin. Struct. Biol. 10, 744–752.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 5
    • 0028874533 scopus 로고
    • Freeze trapping of reaction intermediates
    • Schmidt, K. and Henderson, R. (1995) Freeze trapping of reaction intermediates. Curr. Opin. Struct. Biol. 5, 656–663.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 656-663
    • Schmidt, K.1    Henderson, R.2
  • 6
    • 0035354587 scopus 로고    scopus 로고
    • Time-resolved biochemical crystallography: a mechanistic perspective
    • Schmidt, K. (2001) Time-resolved biochemical crystallography: a mechanistic perspective. Chem. Rev. 101, 1569–1581.
    • (2001) Chem. Rev , vol.101 , pp. 1569-1581
    • Schmidt, K.1
  • 7
    • 0024528771 scopus 로고
    • Time-resolved macromolecular crystallography
    • Schmidt, K. (1989) Time-resolved macromolecular crystallography. Annu. Rev. Biophys. Biophys. Chem. 18, 309–332.
    • (1989) Annu. Rev. Biophys. Biophys. Chem , vol.18 , pp. 309-332
    • Schmidt, K.1
  • 8
    • 0033961309 scopus 로고    scopus 로고
    • Observation of unstable species in enzyme-catalyzed transformations using protein crystallography
    • Petsko, G. A. and Ringe, D. (2000) Observation of unstable species in enzyme-catalyzed transformations using protein crystallography. Curr. Opin. Chem Biol. 4, 89–94.
    • (2000) Curr. Opin. Chem Biol , vol.4 , pp. 89-94
    • Petsko, G. A.1    Ringe, D.2
  • 10
    • 0027191459 scopus 로고
    • Fast crystallography and time-resolved structures
    • Hajdu, J. and Andersson, I. (1993) Fast crystallography and time-resolved structures. Annu. Rev. Biophys. Biomol. Struct. 22, 467–498.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 467-498
    • Hajdu, J.1    Andersson, I.2
  • 11
    • 0029645585 scopus 로고
    • Direct measurement of reactivity in the protein crystal by steady-state kinetic studies
    • Stoddard, B. L. and Farber, G. K. (1995) Direct measurement of reactivity in the protein crystal by steady-state kinetic studies. Structure 3, 991–996.
    • (1995) Structure , vol.3 , pp. 991-996
    • Stoddard, B. L.1    Farber, G. K.2
  • 12
    • 0001504254 scopus 로고    scopus 로고
    • Macromolecular Cryocrystallography
    • Garman, E. F. and Schneider, T. R. (1997) Macromolecular Cryocrystallography. J. Appl. Cryst. 30, 211–237.
    • (1997) J. Appl. Cryst , vol.30 , pp. 211-237
    • Garman, E. F.1    Schneider, T. R.2
  • 13
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: ligand binding to myoglobin
    • Schlichting, I. and Chu, K. (2000) Trapping intermediates in the crystal: ligand binding to myoglobin. Curr. Opin. Struct. Biol. 10, 744–752.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 14
    • 0029645585 scopus 로고
    • Direct measurement of reactivity in the protein crystal by steady-state kinetic studies
    • Stoddard, B. L. and Farber, G. K. (1995) Direct measurement of reactivity in the protein crystal by steady-state kinetic studies. Structure 3, 991–996.
    • (1995) Structure , vol.3 , pp. 991-996
    • Stoddard, B. L.1    Farber, G. K.2
  • 15
    • 0028258783 scopus 로고
    • On the photochemical release of phosphate from 3,5–dinitrophenyl phosphate in a protein crystal
    • Hadfield, A. and Hajdu, J. (1994) On the photochemical release of phosphate from 3,5–dinitrophenyl phosphate in a protein crystal. J. Mol. Biol. 236, 995– 1000.
    • (1994) J. Mol. Biol , vol.236 , pp. 995-1000
    • Hadfield, A.1    Hajdu, J.2
  • 16
    • 0030852353 scopus 로고    scopus 로고
    • Triggering methods in kinetic crystallography
    • Schlichting, I. and Goody, R. (1997) Triggering methods in kinetic crystallography. Methods in Enzymology 277, 467–490.
    • (1997) Methods in Enzymology , vol.277 , pp. 467-490
    • Schlichting, I.1    Goody, R.2
  • 17
    • 0001708188 scopus 로고
    • Direct measurement of diffusion rates in enzyme crystals by video absorbance spectroscopy
    • Ohara, P., Goodwin, P., and Stoddard, B. L. (1995) Direct measurement of diffusion rates in enzyme crystals by video absorbance spectroscopy. J. Appl. Cryst. 28, 829–834.
    • (1995) J. Appl. Cryst , vol.28 , pp. 829-834
    • Ohara, P.1    Goodwin, P.2    Stoddard, B. L.3
  • 18
    • 0029645585 scopus 로고
    • Direct measurement of reactivity in the protein crystal by steady-state kinetic studies
    • Stoddard, B. L. and Farber, G. K. (1995) Direct measurement of reactivity in the protein crystal by steady-state kinetic studies. Structure 3, 991–996.
    • (1995) Structure , vol.3 , pp. 991-996
    • Stoddard, B. L.1    Farber, G. K.2
  • 19
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren, K. H., Seljee, F., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1993) Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363, 693–698.
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K. H.1    Seljee, F.2    Rozeboom, H. J.3    Kalk, K. H.4    Dijkstra, B. W.5
  • 20
    • 0027411179 scopus 로고
    • The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography
    • Singer, P. T., Smalas, A., Carty, R. P., Mangel, W. F., and Sweet, R. M. (1993) The hydrolytic water molecule in trypsin, revealed by time-resolved Laue crystallography. Science 259, 669–673.
    • (1993) Science , vol.259 , pp. 669-673
    • Singer, P. T.1    Smalas, A.2    Carty, R. P.3    Mangel, W. F.4    Sweet, R. M.5
  • 21
    • 0022307510 scopus 로고
    • Diffraction methods for biological macromolecules. Flow cell construction and use
    • Petsko, G. A. (1985) Diffraction methods for biological macromolecules. Flow cell construction and use. Methods Enzymol. 114, 141–146.
    • (1985) Methods Enzymol , vol.114 , pp. 141-146
    • Petsko, G. A.1
  • 22
    • 0021187796 scopus 로고
    • Proteins at work: “stop-action”pictures at subzero temperatures
    • Douzou, P. and Petsko, G. A. (1984) Proteins at work: “stop-action”pictures at subzero temperatures. Adv. Protein Chem 36, 245–361.
    • (1984) Adv. Protein Chem , vol.36 , pp. 245-361
    • Douzou, P.1    Petsko, G. A.2
  • 24
    • 0020842817 scopus 로고
    • Cryoenzymology
    • Douzou, P. (1983) Cryoenzymology. Cryobiology 20, 625–635.
    • (1983) Cryobiology , vol.20 , pp. 625-635
    • Douzou, P.1
  • 26
    • 0029859337 scopus 로고    scopus 로고
    • Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy
    • Gouet, P., Jouve, H. M., Williams, P. A., Andersson, I., Andreoletti, P., Nussaume, L., and Hajdu, J. (1996) Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy. Nat. Struct. Biol. 3, 951–956.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 951-956
    • Gouet, P.1    Jouve, H. M.2    Williams, P. A.3    Andersson, I.4    Andreoletti, P.5    Nussaume, L.6    Hajdu, J.7
  • 27
    • 0031453084 scopus 로고    scopus 로고
    • Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase
    • Jouve, H. M., Andreoletti, P., Gouet, P., Hajdu, J., and Gagnon, J. (1997) Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase. Biochimie 79, 667–671.
    • (1997) Biochimie , vol.79 , pp. 667-671
    • Jouve, H. M.1    Andreoletti, P.2    Gouet, P.3    Hajdu, J.4    Gagnon, J.5
  • 28
    • 0011761816 scopus 로고
    • Cryoenzymology in mixed solvents without cosolvent effects on enzyme specific activity
    • Douzou, P. and Balny, C. (1977) Cryoenzymology in mixed solvents without cosolvent effects on enzyme specific activity. Proc. Natl. Acad. Sci. USA 74, 2297–2300.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2297-2300
    • Douzou, P.1    Balny, C.2
  • 29
    • 0026720247 scopus 로고
    • Crystalline ribonuclease A loses function below the dynamical transition at 220 K
    • Rasmussen, B. F., Stock, A. M., Ringe, D., and Petsko, G. A. (1992) Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 357, 423–424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B. F.1    Stock, A. M.2    Ringe, D.3    Petsko, G. A.4
  • 30
    • 0033554845 scopus 로고    scopus 로고
    • Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate
    • 480
    • Weyand, M. and Schlichting, I. (1999) Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate. Biochemistry 38, 16,469–16,480.
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 469-16
    • Weyand, M.1    Schlichting, I.2
  • 31
    • 0029861873 scopus 로고    scopus 로고
    • Caught in a chemical trap
    • Stoddard, B. L. (1996) Caught in a chemical trap. Nat. Struct. Biol. 3, 907–909.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 907-909
    • Stoddard, B. L.1
  • 32
    • 0034851478 scopus 로고    scopus 로고
    • Trapping reaction intermediates in macromolecular crystals for structural analyses
    • Stoddard, B. L. (2001) Trapping reaction intermediates in macromolecular crystals for structural analyses. Methods 24, 125–138.
    • (2001) Methods , vol.24 , pp. 125-138
    • Stoddard, B. L.1
  • 33
    • 0029777433 scopus 로고    scopus 로고
    • Intermediate trapping and laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening
    • Stoddard, B. L. (1996) Intermediate trapping and laue X-ray diffraction: potential for enzyme mechanism, dynamics, and inhibitor screening. Pharmacol. Ther. 70, 215–256.
    • (1996) Pharmacol. Ther , vol.70 , pp. 215-256
    • Stoddard, B. L.1
  • 34
    • 84971688615 scopus 로고
    • The study of enzyme mechanisms by a combination of cosolvent, low-temperature and high-pressure techniques
    • Douzou, P. (1979) The study of enzyme mechanisms by a combination of cosolvent, low-temperature and high-pressure techniques. Q. Rev. Biophys. 12, 78.
    • (1979) Q. Rev. Biophys , vol.12 , pp. 78
    • Douzou, P.1
  • 35
    • 0028874533 scopus 로고
    • Freeze trapping of reaction intermediates
    • Schmidt, K. and Henderson, R. (1995) Freeze trapping of reaction intermediates. Curr. Opin. Struct. Biol. 5, 656–663.
    • (1995) Curr. Opin. Struct. Biol , vol.5 , pp. 656-663
    • Schmidt, K.1    Henderson, R.2
  • 36
    • 15444378854 scopus 로고
    • X-ray crystallography at extremely low temperatures
    • Schmidt, K. (1995) X-ray crystallography at extremely low temperatures. Biotechnology (N. Y. ) 13, 133.
    • (1995) Biotechnology (N. Y. ) , vol.13 , pp. 133
    • Schmidt, K.1
  • 37
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: ligand binding to myoglobin
    • Schlichting, I. and Chu, K. (2000) Trapping intermediates in the crystal: ligand binding to myoglobin. Curr. Opin. Struct. Biol. 10, 744–752.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 39
  • 40
    • 0033860560 scopus 로고    scopus 로고
    • Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction
    • Murray, J. B., Szoke, H., Szoke, A., and Scott, W. G. (2000) Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction. Mol. Cell 5, 279–287.
    • (2000) Mol. Cell , vol.5 , pp. 279-287
    • Murray, J. B.1    Szoke, H.2    Szoke, A.3    Scott, W. G.4
  • 41
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke, H., Schobert, B., Richter, H. T., Cartailler, J. P., and Lanyi, J. K. (1999) Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 286, 255–261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H. T.3    Cartailler, J. P.4    Lanyi, J. K.5
  • 43
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2000) Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature 406, 645–648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E. M.5    Neutze, R.6
  • 44
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass, H. J., Buldt, G., Gessenich, R., Hehn, D., Neff, D., Schlesinger, R., Berendzen, J., and Ormos, P. (2000) Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature 406, 649–653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H. J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5    Schlesinger, R.6    Berendzen, J.7    Ormos, P.8
  • 46
  • 48
    • 0033988125 scopus 로고    scopus 로고
    • Solvent mobility and the protein ‘glass’ transition
    • Vitkup, D., Ringe, D., Petsko, G. A., and Karplus, M. (2000) Solvent mobility and the protein ‘glass’ transition. Nat. Struct. Biol. 7, 34–38.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 34-38
    • Vitkup, D.1    Ringe, D.2    Petsko, G. A.3    Karplus, M.4
  • 49
    • 0035814133 scopus 로고    scopus 로고
    • Cryophotolysis of ortho-nitrobenzyl derivatives of enzyme ligands for the potential kinetic crystallography of macromolecules
    • Specht, A., Ursby, T., Weik, M., Peng, L., Kroon, J., Bourgeois, D., and Goeldner, M. (2001) Cryophotolysis of ortho-nitrobenzyl derivatives of enzyme ligands for the potential kinetic crystallography of macromolecules. Chembiochem. 2, 845–848.
    • (2001) Chembiochem , vol.2 , pp. 845-848
    • Specht, A.1    Ursby, T.2    Weik, M.3    Peng, L.4    Kroon, J.5    Bourgeois, D.6    Goeldner, M.7
  • 52
    • 0034632821 scopus 로고    scopus 로고
    • Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin
    • Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2000) Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin. Nature 406, 645–648.
    • (2000) Nature , vol.406 , pp. 645-648
    • Royant, A.1    Edman, K.2    Ursby, T.3    Pebay-Peyroula, E.4    Landau, E. M.5    Neutze, R.6
  • 53
  • 54
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • Ostermann, A., Waschipky, R., Parak, F. G., and Nienhaus, G. U. (2000) Ligand binding and conformational motions in myoglobin. Nature 404, 205–208.
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F. G.3    Nienhaus, G. U.4
  • 55
    • 0033961309 scopus 로고    scopus 로고
    • Observation of unstable species in enzyme-catalyzed transformations using protein crystallography
    • Petsko, G. A. and Ringe, D. (2000) Observation of unstable species in enzyme-catalyzed transformations using protein crystallography. Curr. Opin. Chem Biol. 4, 89–94.
    • (2000) Curr. Opin. Chem Biol , vol.4 , pp. 89-94
    • Petsko, G. A.1    Ringe, D.2
  • 56
    • 0033857394 scopus 로고    scopus 로고
    • Crystallographic structure determination of unstable species
    • Schlichting, I. (2000) Crystallographic structure determination of unstable species. Acc. Chem Res. 33, 532–538.
    • (2000) Acc. Chem Res , vol.33 , pp. 532-538
    • Schlichting, I.1
  • 57
    • 0141560454 scopus 로고    scopus 로고
    • The ‘glass transition’ in protein dynamics: what it is, why it occurs, and how to exploit it
    • Ringe, D. and Petsko, G. A. (2003) The ‘glass transition’ in protein dynamics: what it is, why it occurs, and how to exploit it. Biophys. Chem 105, 667–680.
    • (2003) Biophys. Chem , vol.105 , pp. 667-680
    • Ringe, D.1    Petsko, G. A.2
  • 58
    • 0033571343 scopus 로고    scopus 로고
    • The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins
    • Scheidig, A. J., Burmester, C., and Goody, R. S. (1999) The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure Fold. Des 7, 1311–1324.
    • (1999) Structure Fold. Des , vol.7 , pp. 1311-1324
    • Scheidig, A. J.1    Burmester, C.2    Goody, R. S.3


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