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Volumn 36, Issue 3, 1999, Pages 282-294

X-ray crystallographic studies of the denaturation of ribonuclease S

Author keywords

B factors; Crosslinking; Low pH; RNase; Urea

Indexed keywords

GLUTARALDEHYDE; RIBONUCLEASE; RIBONUCLEASE A; UREA;

EID: 0033566805     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990815)36:3<282::AID-PROT3>3.0.CO;2-F     Document Type: Article
Times cited : (17)

References (70)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim PS, Baldwin RL. Intermediates in the folding reactions of small proteins. Ann Rev Biochem 1990;59:631-660.
    • (1990) Ann Rev Biochem , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 0018588511 scopus 로고
    • Stability of proteins
    • Privalov PL. Stability of proteins. Adv Protein Chem 1979;33:167-241.
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 3
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guinea pig α-lactalbumin: A hydrogen exchange study
    • Chayan C, Wormald C, Dobson CM, Evans PA, Baum J. Structure and stability of the molten globule state of guinea pig α-lactalbumin: a hydrogen exchange study. Biochemistry 1993;32:5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chayan, C.1    Wormald, C.2    Dobson, C.M.3    Evans, P.A.4    Baum, J.5
  • 4
    • 0028297302 scopus 로고
    • Structural characterization of the FK506 binding protein unfolded in urea and guanidine chloride
    • Logan TM, Theriault Y, Fesik SW. Structural characterization of the FK506 binding protein unfolded in urea and guanidine chloride. J Mol Biol 1994;236:637-648.
    • (1994) J Mol Biol , vol.236 , pp. 637-648
    • Logan, T.M.1    Theriault, Y.2    Fesik, S.W.3
  • 5
    • 0028466243 scopus 로고
    • Protein folding. Solid evidence for molten globules
    • Dobson CM. Protein folding. Solid evidence for molten globules. Curr Biol 1994;4:636-640.
    • (1994) Curr Biol , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 7
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle DR. Structural analysis of non-native states of proteins by NMR methods. Curr Opin Struct Biol 1996;6:24-30.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 8
    • 0027955640 scopus 로고
    • NMR assignments as a basis for structural characterization of denatured states of globular proteins
    • Wuthrich K. NMR assignments as a basis for structural characterization of denatured states of globular proteins. Curr Opin Struct Biol 1994;4:93-99.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 93-99
    • Wuthrich, K.1
  • 9
    • 0028119049 scopus 로고
    • Specificity of urea binding to proteins
    • Liepinsh E, Otting G. Specificity of urea binding to proteins. J Am Chem Soc 1994;116:9670-9674.
    • (1994) J Am Chem Soc , vol.116 , pp. 9670-9674
    • Liepinsh, E.1    Otting, G.2
  • 10
    • 0029028428 scopus 로고
    • Interaction of urea with unfolded DNA-binding domain of 434 represser
    • Dotsch V, Wider G, Siegal G, Wutrich K. Interaction of urea with unfolded DNA-binding domain of 434 represser. FEBS Lett 1995; 366:6-10.
    • (1995) FEBS Lett , vol.366 , pp. 6-10
    • Dotsch, V.1    Wider, G.2    Siegal, G.3    Wutrich, K.4
  • 11
    • 0026612647 scopus 로고
    • 1H NMR studies of the interaction of urea with hen lysozyme
    • Lumb KJ, Dobson CM. 1H NMR studies of the interaction of urea with hen lysozyme. J Mol Biol 1992;227:9-14.
    • (1992) J Mol Biol , vol.227 , pp. 9-14
    • Lumb, K.J.1    Dobson, C.M.2
  • 12
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidium chloride. Acalorimetric study
    • Makhatadze GI, Privalov PL. Protein interactions with urea and guanidium chloride. Acalorimetric study. J Mol Biol 1992;224:491-505.
    • (1992) J Mol Biol , vol.224 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 13
    • 0015950174 scopus 로고
    • Partial specific volumes and interaction with solvent components of proteins in GuHCl
    • Lee S, Timasheff S. Partial specific volumes and interaction with solvent components of proteins in GuHCl. Biochemistry 1974;13: 257-265.
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, S.1    Timasheff, S.2
  • 15
    • 0015218157 scopus 로고
    • Studies of hydrogen exchange in proteins. VI. Urea effects on ribonuclease exchange kinetics leading to a general model for hydrogen exchange from folded proteins
    • Woodward CK, Rosenberg A. Studies of hydrogen exchange in proteins. VI. Urea effects on ribonuclease exchange kinetics leading to a general model for hydrogen exchange from folded proteins. J Biol Chem 1971;240:4114-4121.
    • (1971) J Biol Chem , vol.240 , pp. 4114-4121
    • Woodward, C.K.1    Rosenberg, A.2
  • 16
    • 0020493395 scopus 로고
    • Hydrogen exchange and the dynamic structure of proteins
    • Woodward C, Simon I, Tuchsen E. Hydrogen exchange and the dynamic structure of proteins. Mol Cell Biochem 1982;48:135-160.
    • (1982) Mol Cell Biochem , vol.48 , pp. 135-160
    • Woodward, C.1    Simon, I.2    Tuchsen, E.3
  • 17
    • 0027394285 scopus 로고
    • Pulsed H/D exchange of folding intermediates
    • Baldwin RL. Pulsed H/D exchange of folding intermediates. Curr Opin Struct Biol 1993;3:84-91.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 84-91
    • Baldwin, R.L.1
  • 19
    • 0027730340 scopus 로고
    • Guanidium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo SL, Baldwin RL. Guanidium chloride induction of partial unfolding in amide proton exchange in RNase A. Science 1993;262: 873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 20
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability, effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim KS, Woodward C. Protein internal flexibility and global stability, effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 1993;32:9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.S.1    Woodward, C.2
  • 21
    • 0028220369 scopus 로고
    • A structural basis for the interaction of urea with lysozyme
    • Pike ACW, Acharya RK. A structural basis for the interaction of urea with lysozyme. Protein Sci 1994;3:706-710.
    • (1994) Protein Sci , vol.3 , pp. 706-710
    • Pike, A.C.W.1    Acharya, R.K.2
  • 23
    • 0027418705 scopus 로고
    • Urea diketopiperizine interactions: A model for urea induced denaturation of proteins
    • Sijpkes AH, Van deKleut G, Gill SC. Urea diketopiperizine interactions: a model for urea induced denaturation of proteins. Biophys Chem 1993;46:171-177.
    • (1993) Biophys Chem , vol.46 , pp. 171-177
    • Sijpkes, A.H.1    Van DeKleut, G.2    Gill, S.C.3
  • 26
    • 0030755707 scopus 로고    scopus 로고
    • CLEC's: Efficient and stable biocatalysts for preparative organic chemistry
    • Zelinski T, Waldmann H. CLEC's: efficient and stable biocatalysts for preparative organic chemistry. Agnew Chem Int Ed Engl 1997;36:722-724.
    • (1997) Agnew Chem Int Ed Engl , vol.36 , pp. 722-724
    • Zelinski, T.1    Waldmann, H.2
  • 27
    • 0018266792 scopus 로고
    • Crystal structures of chymotrypsin in GuHCl and urea
    • Hibbard LS, Tulinsky A. Crystal structures of chymotrypsin in GuHCl and urea. Biochemistry 1978;17:5460-5468.
    • (1978) Biochemistry , vol.17 , pp. 5460-5468
    • Hibbard, L.S.1    Tulinsky, A.2
  • 28
    • 0017363495 scopus 로고
    • Crystallographic studies of protein denaturation and renaturation 1. Effects of denaturants on volume and X-ray pattern of cross-linked lysozyme crystals
    • Yonath A, Sielecki A, Moult J, Podjarny A, Traub W. Crystallographic studies of protein denaturation and renaturation 1. Effects of denaturants on volume and X-ray pattern of cross-linked lysozyme crystals. Biochemistry 1977;16:1413-1417.
    • (1977) Biochemistry , vol.16 , pp. 1413-1417
    • Yonath, A.1    Sielecki, A.2    Moult, J.3    Podjarny, A.4    Traub, W.5
  • 29
    • 0017335799 scopus 로고
    • Crystallographic studies of protein denaturation and renaturation 2. Sodium dodecyl induced structural changes in triclinic lysozyme
    • Yonath A, Podjarny A, Honig B, Sielecki A, Traub W. Crystallographic studies of protein denaturation and renaturation 2. Sodium dodecyl induced structural changes in triclinic lysozyme Biochemistry 1977;16:1418-1424.
    • (1977) Biochemistry , vol.16 , pp. 1418-1424
    • Yonath, A.1    Podjarny, A.2    Honig, B.3    Sielecki, A.4    Traub, W.5
  • 30
    • 0016345765 scopus 로고
    • Crystallographic study of the interaction of urea with lysozyme
    • Snape KW, Tijan R, Blake CCF, Koshland DE, Jr. Crystallographic study of the interaction of urea with lysozyme. Nature 1974;250:294-298.
    • (1974) Nature , vol.250 , pp. 294-298
    • Snape, K.W.1    Tijan, R.2    Blake, C.C.F.3    Koshland D.E., Jr.4
  • 31
    • 0022555882 scopus 로고
    • Complementation in folding and fragment exchange
    • Taniuchi HT, Parr GR, Juillerat MA. Complementation in folding and fragment exchange. Meth Enzymol 1986;131:185-217.
    • (1986) Meth Enzymol , vol.131 , pp. 185-217
    • Taniuchi, H.T.1    Parr, G.R.2    Juillerat, M.A.3
  • 32
    • 84965093921 scopus 로고
    • The preparation of subtilisin modified ribonuclease and the separation of its peptide and protein components
    • Richards FM, Vithayathil PJ. The preparation of subtilisin modified ribonuclease and the separation of its peptide and protein components. J Biol Chem 1959;234:1459-1464.
    • (1959) J Biol Chem , vol.234 , pp. 1459-1464
    • Richards, F.M.1    Vithayathil, P.J.2
  • 33
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • Richards FM, Wyckoff HW. Bovine pancreatic ribonuclease. The Enzymes 1971;4:647-806.
    • (1971) The Enzymes , vol.4 , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.W.2
  • 34
    • 77956940788 scopus 로고
    • Pancreatic ribonuclease
    • Blackburn P, Moore S. Pancreatic ribonuclease. The Enzymes 1982;15:317-433.
    • (1982) The Enzymes , vol.15 , pp. 317-433
    • Blackburn, P.1    Moore, S.2
  • 35
    • 0025293251 scopus 로고
    • Thermodynamics of protein-peptide interactions in the ribonuclease-S system studied by titration calorimetry
    • Connelly PR, Varadarajan R, Sturtevant JM, Richards FM Thermodynamics of protein-peptide interactions in the ribonuclease-S system studied by titration calorimetry. Biochemistry 1990; 29:6108-6114.
    • (1990) Biochemistry , vol.29 , pp. 6108-6114
    • Connelly, P.R.1    Varadarajan, R.2    Sturtevant, J.M.3    Richards, F.M.4
  • 36
    • 0029912028 scopus 로고    scopus 로고
    • Dynamics of ribonuclease A and ribonuclease S: Computational and experimental studies
    • Nadig G, Ratnaparkhi GS, Varadarajan R, Vishveshwara S. Dynamics of ribonuclease A and ribonuclease S: Computational and experimental studies. Protein Sci 1996;5:2104-2114.
    • (1996) Protein Sci , vol.5 , pp. 2104-2114
    • Nadig, G.1    Ratnaparkhi, G.S.2    Varadarajan, R.3    Vishveshwara, S.4
  • 37
    • 0026999215 scopus 로고
    • Refinement of the crystal structures of ribonuclease S. Comparison with and between the various ribonuclease A structures
    • Kim EE, Varadarajan R, Wyckoff HW, Richards FM. Refinement of the crystal structures of ribonuclease S. Comparison with and between the various ribonuclease A structures. Biochemistry 1992;31:12304-12314.
    • (1992) Biochemistry , vol.31 , pp. 12304-12314
    • Kim, E.E.1    Varadarajan, R.2    Wyckoff, H.W.3    Richards, F.M.4
  • 38
    • 0028197609 scopus 로고
    • Interaction of semisynthetic variants of RNase A with ribonuclease inhibitor
    • Neumann U, Hofstengee J. Interaction of semisynthetic variants of RNase A with ribonuclease inhibitor. Protein Sci 1994;3:248-256.
    • (1994) Protein Sci , vol.3 , pp. 248-256
    • Neumann, U.1    Hofstengee, J.2
  • 39
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton, TE, editor. IRL Press: Oxford
    • Pace CN, Shirley BA, Thomson JA. Measuring the conformational stability of a protein. In: Creighton, TE, editor. Protein structure, a practical approach. IRL Press: Oxford; 1990. p 311-329.
    • (1990) Protein Structure, a Practical Approach , pp. 311-329
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 40
    • 78651149328 scopus 로고
    • Intermolecular crosslinking of a protein in the crystalline state: Carboxypeptidase A
    • Quiocho FA, Richards FM. Intermolecular crosslinking of a protein in the crystalline state: carboxypeptidase A. Proc Natl Acad Sci USA 1964;52:833-839.
    • (1964) Proc Natl Acad Sci USA , vol.52 , pp. 833-839
    • Quiocho, F.A.1    Richards, F.M.2
  • 41
    • 0014414239 scopus 로고
    • Glutaraldehyde as a protein crosslinking agent
    • Richards FM, Knowles J. Glutaraldehyde as a protein crosslinking agent. J Mol Biol 1968;37:231-233.
    • (1968) J Mol Biol , vol.37 , pp. 231-233
    • Richards, F.M.1    Knowles, J.2
  • 42
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch WJ. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. Appl Cryst 1993;26:795-800.
    • (1993) Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.J.1
  • 44
    • 0026597444 scopus 로고
    • The Free R Value: A novel statistical quantity for assessing the accuracy of a crystal structure
    • Brunger AT. The Free R Value: A novel statistical quantity for assessing the accuracy of a crystal structure. Nature 1992;355:472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 45
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination. Applications of the free R value
    • Kleywegt GJ, Brunger AT. Checking your imagination. Applications of the free R value. Structure 1996;4:897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brunger, A.T.2
  • 46
    • 0028070557 scopus 로고
    • Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
    • Rice LM, Brunger AT. Torsion angle dynamics: reduced variable conformational sampling enhances crystallographic structure refinement. Proteins 1994;19:277-290.
    • (1994) Proteins , vol.19 , pp. 277-290
    • Rice, L.M.1    Brunger, A.T.2
  • 47
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of chaperonin GroEL at 2.8 Å
    • Braig K, Adams PD, Brunger AT. Conformational variability in the refined structure of chaperonin GroEL at 2.8 Å. Nat Struct Biol 1995;2:1083-1094.
    • (1995) Nat Struct Biol , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brunger, A.T.3
  • 48
    • 84944812409 scopus 로고
    • Improved fourier coefficient for maps using phases from partial structure with errors
    • Read RJ. Improved fourier coefficient for maps using phases from partial structure with errors. Acta Crystallogr A 1986;42:140-149.
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 49
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones TA. Interactive computer graphics: FRODO. Meth Enzymol 1985;115:157-171.
    • (1985) Meth Enzymol , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 50
    • 0025148114 scopus 로고
    • Incorporation of crystallographic temperature factors in the statistical analysis of protein tertiary structures
    • Bott R, Frane J. Incorporation of crystallographic temperature factors in the statistical analysis of protein tertiary structures. Protein Eng 1990;3:649-657.
    • (1990) Protein Eng , vol.3 , pp. 649-657
    • Bott, R.1    Frane, J.2
  • 51
    • 0021107965 scopus 로고
    • Solvent accessible surfaces of proteins and nucleic acids
    • Connolly ML. Solvent accessible surfaces of proteins and nucleic acids. Science 1983;221:709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 52
    • 0029411262 scopus 로고
    • Occluded molecular surface: An analysis of protein packing
    • Pattabiraman N, Ward KB, Fleming PJ. Occluded molecular surface: an analysis of protein packing. J Mol Recog 1995;8:334-344.
    • (1995) J Mol Recog , vol.8 , pp. 334-344
    • Pattabiraman, N.1    Ward, K.B.2    Fleming, P.J.3
  • 54
    • 0032510813 scopus 로고    scopus 로고
    • Discrepancies between the X-ray and NMR structures of uncomplexed barstar. Analysis suggests that protein density is not well determined by NMR
    • Ratnaparkhi GS, Ramachandran S, Udgaonkar JB, Varadarajan R. Discrepancies between the X-ray and NMR structures of uncomplexed barstar. Analysis suggests that protein density is not well determined by NMR. Biochemistry 1998;36:6958-6966.
    • (1998) Biochemistry , vol.36 , pp. 6958-6966
    • Ratnaparkhi, G.S.1    Ramachandran, S.2    Udgaonkar, J.B.3    Varadarajan, R.4
  • 55
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 1993;26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0025865081 scopus 로고
    • Comparison of structures of dry and wet egg-white lysozyme molecule at 1.8 Å
    • Kachalokova S, Morozov VN, Morozova YY, et al. Comparison of structures of dry and wet egg-white lysozyme molecule at 1.8 Å. FEBS Lett 1991;284:91-94.
    • (1991) FEBS Lett , vol.284 , pp. 91-94
    • Kachalokova, S.1    Morozov, V.N.2    Morozova, Y.Y.3
  • 58
    • 0028304966 scopus 로고
    • X-ray structure of a cross-linked subtilisin Carlsberg in water vs acetonitrile
    • Fitzpatrick PA, Ringe D, Klibanov A.M. X-ray structure of a cross-linked subtilisin Carlsberg in water vs acetonitrile. Biophys Biochem Res Commun 1994;198:675-681.
    • (1994) Biophys Biochem Res Commun , vol.198 , pp. 675-681
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3
  • 59
    • 0017420380 scopus 로고
    • Reactivity and cryoenzymology of enzymes in the crystalline state
    • Maniken MW, Fink AL. Reactivity and cryoenzymology of enzymes in the crystalline state. Ann Rev Biophys Bioeng 1977;6: 301-343.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 301-343
    • Maniken, M.W.1    Fink, A.L.2
  • 60
    • 0027953901 scopus 로고
    • Structural characterization of a three disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways
    • Talluri S, Rothwarf DW, Scheraga HA. Structural characterization of a three disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways. Biochemistry 1994;33: 10437-10449.
    • (1994) Biochemistry , vol.33 , pp. 10437-10449
    • Talluri, S.1    Rothwarf, D.W.2    Scheraga, H.A.3
  • 61
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 1994;33:12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 62
  • 63
    • 0031032512 scopus 로고    scopus 로고
    • Probing subtle acid-induced conformational changes of ribonuclease A by elctrospray mass spectroscopy
    • Pan XM, Sheng XR, Yang SM, Zhou JM. Probing subtle acid-induced conformational changes of ribonuclease A by elctrospray mass spectroscopy. FEBS Lett 1997;402:25-27.
    • (1997) FEBS Lett , vol.402 , pp. 25-27
    • Pan, X.M.1    Sheng, X.R.2    Yang, S.M.3    Zhou, J.M.4
  • 64
    • 0026998178 scopus 로고
    • Crystallographic structures of ribonuclease S variants with nonpolar substitutions at position 13: Packing and cavities
    • Varadarajan R, Richards FM. Crystallographic structures of ribonuclease S variants with nonpolar substitutions at position 13: packing and cavities. Biochemistry 1992;31:12313-12327.
    • (1992) Biochemistry , vol.31 , pp. 12313-12327
    • Varadarajan, R.1    Richards, F.M.2
  • 65
    • 0008426602 scopus 로고
    • Limited digestion of ribonuclease with pepsin
    • Anfinsen CB. Limited digestion of ribonuclease with pepsin. J Biol Chem 1956;221:405-415.
    • (1956) J Biol Chem , vol.221 , pp. 405-415
    • Anfinsen, C.B.1
  • 66
    • 0345115202 scopus 로고
    • Structural studies of ribonuclease. XVIII. An investigation of the peptic digestion products of ribonuclease
    • Fujioka H, Scheraga HA. Structural studies of ribonuclease. XVIII. An investigation of the peptic digestion products of ribonuclease. Biochemistry 1965;4:2197-2205.
    • (1965) Biochemistry , vol.4 , pp. 2197-2205
    • Fujioka, H.1    Scheraga, H.A.2
  • 67
    • 0030833143 scopus 로고    scopus 로고
    • Synchrotron radiation applications to macromolecular crystallography
    • Moffat K, Zong R. Synchrotron radiation applications to macromolecular crystallography. Curr Opin Struct Biol 1997;7:689-696.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 689-696
    • Moffat, K.1    Zong, R.2
  • 68
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental Crystallographic phases
    • Burling FT, Weis WI, Flaherty KM, Brunger AT. Direct observation of protein solvation and discrete disorder with experimental Crystallographic phases. Science 1996;271:72-76.
    • (1996) Science , vol.271 , pp. 72-76
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 69
    • 0030783379 scopus 로고    scopus 로고
    • Phasing methods for protein crystallography
    • Hauptmann H. Phasing methods for protein crystallography. Curr Opin Struct Biol 1997;7:672-680.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 672-680
    • Hauptmann, H.1


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