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Volumn 15, Issue 5, 2005, Pages 538-547

Advances in kinetic protein crystallography

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN; PHOTOACTIVE YELLOW PROTEIN;

EID: 25844521524     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.08.002     Document Type: Review
Times cited : (116)

References (60)
  • 1
    • 4143061452 scopus 로고    scopus 로고
    • Exploring the structural dynamics of the E. coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states
    • C. Chaudhry, A.L. Horwich, A.T. Brunger, and P.D. Adams Exploring the structural dynamics of the E. coli chaperonin GroEL using translation-libration- screw crystallographic refinement of intermediate states J Mol Biol 342 2004 229 245
    • (2004) J Mol Biol , vol.342 , pp. 229-245
    • Chaudhry, C.1    Horwich, A.L.2    Brunger, A.T.3    Adams, P.D.4
  • 2
    • 0037246863 scopus 로고    scopus 로고
    • MolMovDB: Analysis and visualization of conformational change and structural flexibility
    • N. Echols, D. Milburn, and M. Gerstein MolMovDB: analysis and visualization of conformational change and structural flexibility Nucleic Acids Res 31 2003 478 482
    • (2003) Nucleic Acids Res , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 3
    • 0035354587 scopus 로고    scopus 로고
    • Time-resolved biochemical crystallography: A mechanistic perspective
    • K. Moffat Time-resolved biochemical crystallography: a mechanistic perspective Chem Rev 101 2001 1569 1581
    • (2001) Chem Rev , vol.101 , pp. 1569-1581
    • Moffat, K.1
  • 4
    • 0033961309 scopus 로고    scopus 로고
    • Observation of unstable species in enzyme-catalyzed transformations using protein crystallography
    • G.A. Petsko, and D. Ringe Observation of unstable species in enzyme-catalyzed transformations using protein crystallography Curr Opin Chem Biol 4 2000 89 94
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 89-94
    • Petsko, G.A.1    Ringe, D.2
  • 6
    • 0034519834 scopus 로고    scopus 로고
    • Trapping intermediates in the crystal: Ligand binding to myoglobin
    • I. Schlichting, and K. Chu Trapping intermediates in the crystal: ligand binding to myoglobin Curr Opin Struct Biol 10 2000 744 752
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 744-752
    • Schlichting, I.1    Chu, K.2
  • 7
    • 0141918782 scopus 로고    scopus 로고
    • Proteins in action: The physics of structural fluctuations and conformational changes
    • F.G. Parak Proteins in action: the physics of structural fluctuations and conformational changes Curr Opin Struct Biol 13 2003 552 557
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 552-557
    • Parak, F.G.1
  • 8
    • 0037388383 scopus 로고    scopus 로고
    • Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations
    • S.J. Johnson, J.S. Taylor, and L.S. Beese Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations Proc Natl Acad Sci USA 100 2003 3895 3900 This fascinating paper illustrates the fact that enzymes can be active in the crystalline form. The authors show that crystalline thermostable Bacillus DNA polymerase I is able to elongate a DNA template by up to six bases, generating the largest structural shift observed in a crystal so far.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3895-3900
    • Johnson, S.J.1    Taylor, J.S.2    Beese, L.S.3
  • 9
    • 0344837328 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis thymidylate kinase: Structural studies of intermediates along the reaction pathway
    • E. Fioravanti, A. Haouz, T. Ursby, H. Munier-Lehmann, M. Delarue, and D. Bourgeois Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway J Mol Biol 327 2003 1077 1092
    • (2003) J Mol Biol , vol.327 , pp. 1077-1092
    • Fioravanti, E.1    Haouz, A.2    Ursby, T.3    Munier-Lehmann, H.4    Delarue, M.5    Bourgeois, D.6
  • 10
    • 0037069392 scopus 로고    scopus 로고
    • The catalytic cycle of beta-lactam synthetase observed by X-ray crystallographic snapshots
    • M.T. Miller, B.O. Bachmann, C.A. Townsend, and A.C. Rosenzweig The catalytic cycle of beta-lactam synthetase observed by X-ray crystallographic snapshots Proc Natl Acad Sci USA 99 2002 14752 14757
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14752-14757
    • Miller, M.T.1    Bachmann, B.O.2    Townsend, C.A.3    Rosenzweig, A.C.4
  • 11
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • S. Crosson, and K. Moffat Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch Plant Cell 14 2002 1067 1075
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 12
    • 0037953003 scopus 로고    scopus 로고
    • Capturing enzyme structure prior to reaction initiation: Tropinone reductase-II-substrate complexes
    • A. Yamashita, M. Endo, T. Higashi, T. Nakatsu, Y. Yamada, J. Oda, and H. Kato Capturing enzyme structure prior to reaction initiation: tropinone reductase-II-substrate complexes Biochemistry 42 2003 5566 5573 A careful study based on the 'steady-state' strategy, using conventional Laue diffraction and a flow cell.
    • (2003) Biochemistry , vol.42 , pp. 5566-5573
    • Yamashita, A.1    Endo, M.2    Higashi, T.3    Nakatsu, T.4    Yamada, Y.5    Oda, J.6    Kato, H.7
  • 13
    • 0037154146 scopus 로고    scopus 로고
    • Snapshot of a key intermediate in enzymatic thiamin catalysis: Crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae
    • E. Fiedler, S. Thorell, T. Sandalova, R. Golbik, S. Konig, and G. Schneider Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the alpha-carbanion of (alpha,beta-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae Proc Natl Acad Sci USA 99 2002 591 595
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 591-595
    • Fiedler, E.1    Thorell, S.2    Sandalova, T.3    Golbik, R.4    Konig, S.5    Schneider, G.6
  • 14
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • •] but not in [11], cysteinyl-flavin bond breakage by the X-rays was observed and a composite data set strategy had to be used. A possible explanation for the difference is that the steady-state illumination during data collection in [11] effectively competed with the effects of X-ray-induced photo-electrons.
    • (2003) Biophys J , vol.84 , pp. 2474-2482
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 15
    • 0347264753 scopus 로고    scopus 로고
    • Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
    • A. Karlsson, J.V. Parales, R.E. Parales, D.T. Gibson, H. Eklund, and S. Ramaswamy Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron Science 299 2003 1039 1042 An interesting article describing a fortunate case whereby the 'trigger-freeze' approach could be applied very successfully. In a previous paper, the authors had noticed reduction of the enzyme's Rieske iron-sulfur cluster by X-rays.
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibson, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 17
    • 2442545587 scopus 로고    scopus 로고
    • Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex
    • S.T. Prigge, B.A. Eipper, R.E. Mains, and L.M. Amzel Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex Science 304 2004 864 867
    • (2004) Science , vol.304 , pp. 864-867
    • Prigge, S.T.1    Eipper, B.A.2    Mains, R.E.3    Amzel, L.M.4
  • 18
    • 2542488279 scopus 로고    scopus 로고
    • The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product
    • I. Leiros, S. McSweeney, and E. Hough The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product J Mol Biol 339 2004 805 820
    • (2004) J Mol Biol , vol.339 , pp. 805-820
    • Leiros, I.1    McSweeney, S.2    Hough, E.3
  • 19
    • 2942752112 scopus 로고    scopus 로고
    • Initial events in the photocycle of photoactive yellow protein
    • R. Kort, K.J. Hellingwerf, and R.B. Ravelli Initial events in the photocycle of photoactive yellow protein J Biol Chem 279 2004 26417 26424 The authors used experimental phases from the photoexcited state to avoid model bias in the computation of difference maps for PYP.
    • (2004) J Biol Chem , vol.279 , pp. 26417-26424
    • Kort, R.1    Hellingwerf, K.J.2    Ravelli, R.B.3
  • 20
    • 0036452022 scopus 로고    scopus 로고
    • Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin
    • Y. Matsui, K. Sakai, M. Murakami, Y. Shiro, S. Adachi, H. Okumura, and T. Kouyama Specific damage induced by X-ray radiation and structural changes in the primary photoreaction of bacteriorhodopsin J Mol Biol 324 2002 469 481
    • (2002) J Mol Biol , vol.324 , pp. 469-481
    • Matsui, Y.1    Sakai, K.2    Murakami, M.3    Shiro, Y.4    Adachi, S.5    Okumura, H.6    Kouyama, T.7
  • 22
    • 4444294012 scopus 로고    scopus 로고
    • Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
    • V. Adam, A. Royant, V. Niviere, F.P. Molina-Heredia, and D. Bourgeois Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction Structure 12 2004 1729 1740 The deliberate use of X-ray-induced photo-electrons allowed the authors to visualize subtle elongation of the active site iron-ligand bonds upon reduction. In contrast to [21], composite data sets were collected on a single crystal and microspectrophotometry was used on-line.
    • (2004) Structure , vol.12 , pp. 1729-1740
    • Adam, V.1    Royant, A.2    Niviere, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 23
    • 0038472361 scopus 로고    scopus 로고
    • Direct observation of photolysis-induced tertiary structural changes in hemoglobin
    • S. Adachi, S.Y. Park, J.R. Tame, Y. Shiro, and N. Shibayama Direct observation of photolysis-induced tertiary structural changes in hemoglobin Proc Natl Acad Sci USA 100 2003 7039 7044 Uncommonly large structural changes were observed upon CO photolysis in the T state of hemoglobin at 25-35 K, well below a dynamical transition. This might originate from the fact that the starting CO-bound structure is heavily strained and that photodissociation releases this strain. In this respect, the system is very original.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7039-7044
    • Adachi, S.1    Park, S.Y.2    Tame, J.R.3    Shiro, Y.4    Shibayama, N.5
  • 24
    • 4143105792 scopus 로고    scopus 로고
    • CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: Mechanism of escaping from product inhibition
    • M. Sugishima, H. Sakamoto, M. Noguchi, and K. Fukuyama CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: mechanism of escaping from product inhibition J Mol Biol 341 2004 7 13
    • (2004) J Mol Biol , vol.341 , pp. 7-13
    • Sugishima, M.1    Sakamoto, H.2    Noguchi, M.3    Fukuyama, K.4
  • 25
    • 4644242592 scopus 로고    scopus 로고
    • Structural heterogeneity of cryotrapped intermediates in the bacterial blue light photoreceptor, photoactive yellow protein
    • S. Anderson, V. Srajer, and K. Moffat Structural heterogeneity of cryotrapped intermediates in the bacterial blue light photoreceptor, photoactive yellow protein Photochem Photobiol 80 2004 7 14 The potential complexity of photoexcited cryo-trapped structures is well illustrated by PYP.
    • (2004) Photochem Photobiol , vol.80 , pp. 7-14
    • Anderson, S.1    Srajer, V.2    Moffat, K.3
  • 27
    • 16344386420 scopus 로고    scopus 로고
    • Ligand migration and protein fluctuations in myoglobin mutant L29W
    • K. Nienhaus, A. Ostermann, G.U. Nienhaus, F.G. Parak, and M. Schmidt Ligand migration and protein fluctuations in myoglobin mutant L29W Biochemistry 44 2005 5095 5105 The authors devised an elegant 'freeze-trigger' experiment. Using an appropriate temperature profile, they managed to visualize in detail the recombination steps of CO to Mb. The effect of cooling a protein from 300 K to 110 K is remarkably illustrated by drastic changes in the CO stretch bands from in crystallo FT-IR spectra, which correlate with subtle structural modifications seen in the X-ray data.
    • (2005) Biochemistry , vol.44 , pp. 5095-5105
    • Nienhaus, K.1    Ostermann, A.2    Nienhaus, G.U.3    Parak, F.G.4    Schmidt, M.5
  • 29
    • 0041758430 scopus 로고    scopus 로고
    • Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography
    • D. Bourgeois, B. Vallone, F. Schotte, A. Arcovito, A.E. Miele, G. Sciara, M. Wulff, P. Anfinrud, and M. Brunori Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography Proc Natl Acad Sci USA 100 2003 8704 8709 A step forward in the quality of ultrafast Laue data. Density maps at 1.6 Å resolution revealed extended structural changes upon CO photolysis in an Mb mutant. These changes affect whole secondary structures (helix E, turn CD) and lag 100 ns behind local rearrangements around the heme, which occur promptly.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8704-8709
    • Bourgeois, D.1    Vallone, B.2    Schotte, F.3    Arcovito, A.4    Miele, A.E.5    Sciara, G.6    Wulff, M.7    Anfinrud, P.8    Brunori, M.9
  • 31
    • 4344574384 scopus 로고    scopus 로고
    • Picosecond time-resolved X-ray crystallography: Probing protein function in real time
    • F. Schotte, J. Soman, J.S. Olson, M. Wulff, and P.A. Anfinrud Picosecond time-resolved X-ray crystallography: probing protein function in real time J Struct Biol 147 2004 235 246
    • (2004) J Struct Biol , vol.147 , pp. 235-246
    • Schotte, F.1    Soman, J.2    Olson, J.S.3    Wulff, M.4    Anfinrud, P.A.5
  • 32
    • 1942469425 scopus 로고    scopus 로고
    • Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center
    • R.H. Baxter, N. Ponomarenko, V. Srajer, R. Pahl, K. Moffat, and J.R. Norris Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center Proc Natl Acad Sci USA 101 2004 5982 5987
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5982-5987
    • Baxter, R.H.1    Ponomarenko, N.2    Srajer, V.3    Pahl, R.4    Moffat, K.5    Norris, J.R.6
  • 33
    • 2942533032 scopus 로고    scopus 로고
    • Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein
    • S. Anderson, V. Srajer, R. Pahl, S. Rajagopal, F. Schotte, P. Anfinrud, M. Wulff, and K. Moffat Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein Structure 12 2004 1039 1045
    • (2004) Structure , vol.12 , pp. 1039-1045
    • Anderson, S.1    Srajer, V.2    Pahl, R.3    Rajagopal, S.4    Schotte, F.5    Anfinrud, P.6    Wulff, M.7    Moffat, K.8
  • 35
    • 11844294715 scopus 로고    scopus 로고
    • A structural pathway for signaling in the E46Q mutant of photoactive yellow protein
    • S. Rajagopal, S. Anderson, V. Srajer, M. Schmidt, R. Pahl, and K. Moffat A structural pathway for signaling in the E46Q mutant of photoactive yellow protein Structure 13 2005 55 63 SVD analysis of 54 Laue data sets collected over the past few years provided a convincing structural picture of signaling in the E46Q mutant of PYP. Five distinct structural intermediates were identified and a plausible mechanism for their interconversion is proposed.
    • (2005) Structure , vol.13 , pp. 55-63
    • Rajagopal, S.1    Anderson, S.2    Srajer, V.3    Schmidt, M.4    Pahl, R.5    Moffat, K.6
  • 37
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • H. Frauenfelder, S.G. Sligar, and P.G. Wolynes The energy landscapes and motions of proteins Science 254 1991 1598 1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 38
    • 16244392086 scopus 로고    scopus 로고
    • When X-rays modify the protein structure: Radiation damage at work
    • O. Carugo, and K.D. Carugo When X-rays modify the protein structure: radiation damage at work Trends Biochem Sci 30 2005 213 219
    • (2005) Trends Biochem Sci , vol.30 , pp. 213-219
    • Carugo, O.1    Carugo, K.D.2
  • 39
    • 9944232681 scopus 로고    scopus 로고
    • Microspectrophotometry for structural enzymology
    • A.R. Pearson, A. Mozzarelli, and G.L. Rossi Microspectrophotometry for structural enzymology Curr Opin Struct Biol 14 2004 656 662 A useful review on microspectrophotometry.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 656-662
    • Pearson, A.R.1    Mozzarelli, A.2    Rossi, G.L.3
  • 40
    • 0028898295 scopus 로고
    • Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals
    • K. Ng, E.D. Getzoff, and K. Moffat Optical studies of a bacterial photoreceptor protein, photoactive yellow protein, in single crystals Biochemistry 34 1995 879 890
    • (1995) Biochemistry , vol.34 , pp. 879-890
    • Ng, K.1    Getzoff, E.D.2    Moffat, K.3
  • 43
    • 2142699539 scopus 로고    scopus 로고
    • Temperature derivative fluorescence spectroscopy as a tool to study dynamical changes in protein crystals
    • M. Weik, X. Vernede, A. Royant, and D. Bourgeois Temperature derivative fluorescence spectroscopy as a tool to study dynamical changes in protein crystals Biophys J 86 2004 3176 3185 The authors proposed that exogenous fluorophores can be used to follow solvent glass transitions or protein dynamical transitions within crystals by fluorescence microspectrophotometry.
    • (2004) Biophys J , vol.86 , pp. 3176-3185
    • Weik, M.1    Vernede, X.2    Royant, A.3    Bourgeois, D.4
  • 44
    • 3142658015 scopus 로고    scopus 로고
    • Following ligand binding and ligand reactions in proteins via Raman crystallography
    • P.R. Carey, and J. Dong Following ligand binding and ligand reactions in proteins via Raman crystallography Biochemistry 43 2004 8885 8893
    • (2004) Biochemistry , vol.43 , pp. 8885-8893
    • Carey, P.R.1    Dong, J.2
  • 45
    • 0037452887 scopus 로고    scopus 로고
    • Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray data
    • M. Hogbom, M. Galander, M. Andersson, M. Kolberg, W. Hofbauer, G. Lassmann, P. Nordlund, and F. Lendzian Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray data Proc Natl Acad Sci USA 100 2003 3209 3214
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3209-3214
    • Hogbom, M.1    Galander, M.2    Andersson, M.3    Kolberg, M.4    Hofbauer, W.5    Lassmann, G.6    Nordlund, P.7    Lendzian, F.8
  • 47
    • 0034808210 scopus 로고    scopus 로고
    • Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes
    • M. Weik, R.B. Ravelli, I. Silman, J.L. Sussman, P. Gros, and J. Kroon Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes Protein Sci 10 2001 1953 1961
    • (2001) Protein Sci , vol.10 , pp. 1953-1961
    • Weik, M.1    Ravelli, R.B.2    Silman, I.3    Sussman, J.L.4    Gros, P.5    Kroon, J.6
  • 48
    • 25844516394 scopus 로고    scopus 로고
    • New perspectives in kinetic protein crystallography using caged compounds
    • R. Givens Wiley-vch
    • D. Bourgeois, and M. Weik New perspectives in kinetic protein crystallography using caged compounds R. Givens Dynamic Studies in Biology 2005 Wiley-vch 410 434 If you enjoyed reading our review, take a look at this more detailed book chapter!
    • (2005) Dynamic Studies in Biology , pp. 410-434
    • Bourgeois, D.1    Weik, M.2
  • 49
    • 0035918224 scopus 로고    scopus 로고
    • Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase
    • T. Sjogren, and J. Hajdu Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase J Biol Chem 276 2001 13072 13076
    • (2001) J Biol Chem , vol.276 , pp. 13072-13076
    • Sjogren, T.1    Hajdu, J.2
  • 51
    • 16644374726 scopus 로고    scopus 로고
    • Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data
    • J. Wang, and S.E. Ealick Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data Acta Crystallogr D Biol Crystallogr 60 2004 1579 1585
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1579-1585
    • Wang, J.1    Ealick, S.E.2
  • 54
    • 0037342350 scopus 로고    scopus 로고
    • Application of singular value decomposition to the analysis of time-resolved macromolecular X-ray data
    • M. Schmidt, S. Rajagopal, Z. Ren, and K. Moffat Application of singular value decomposition to the analysis of time-resolved macromolecular X-ray data Biophys J 84 2003 2112 2129
    • (2003) Biophys J , vol.84 , pp. 2112-2129
    • Schmidt, M.1    Rajagopal, S.2    Ren, Z.3    Moffat, K.4
  • 55
    • 11844255732 scopus 로고    scopus 로고
    • Resolving protein structure dynamically
    • S. Yeremenko, and K.J. Hellingwerf Resolving protein structure dynamically Structure 13 2005 4 6
    • (2005) Structure , vol.13 , pp. 4-6
    • Yeremenko, S.1    Hellingwerf, K.J.2
  • 56
    • 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
  • 57
    • 0036101649 scopus 로고    scopus 로고
    • Protein crystallography in a vapour stream: Data collection, reaction initiation and intermediate trapping in naked hydrated protein crystals
    • T. Sjogren, G. Carlsson, G. Larsson, A. Hajdu, C. Andersson, H. Petterssona, and J. Hajdua Protein crystallography in a vapour stream: data collection, reaction initiation and intermediate trapping in naked hydrated protein crystals J Appl Cryst 35 2002 113 116
    • (2002) J Appl Cryst , vol.35 , pp. 113-116
    • Sjogren, T.1    Carlsson, G.2    Larsson, G.3    Hajdu, A.4    Andersson, C.5    Petterssona, H.6    Hajdua, J.7
  • 59
    • 0028801485 scopus 로고
    • Difference refinement: Obtaining differences between two related structures
    • T.C. Terwilliger, and J. Berendzen Difference refinement: obtaining differences between two related structures Acta Crystallogr D Biol Crystallogr 51 1995 609 618
    • (1995) Acta Crystallogr D Biol Crystallogr , vol.51 , pp. 609-618
    • Terwilliger, T.C.1    Berendzen, J.2
  • 60
    • 4344649800 scopus 로고    scopus 로고
    • Potential impact of an X-ray free electron laser on structural biology
    • R. Neutze, G. Huldt, J. Hajdu, and D. van der Spoel Potential impact of an X-ray free electron laser on structural biology Rad Phys Chem 71 2004 905 916
    • (2004) Rad Phys Chem , vol.71 , pp. 905-916
    • Neutze, R.1    Huldt, G.2    Hajdu, J.3    Van Der Spoel, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.