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Volumn 6, Issue 6, 1998, Pages 757-767

Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization

Author keywords

Disulfide bond; DsbA; Protein folding; Protein structure; Thioredoxin fold

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0032526690     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00077-X     Document Type: Article
Times cited : (146)

References (55)
  • 1
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J.L. (1995). Thioredoxin - a fold for all reasons. Structure, 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 2
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C. & Raina, S. (1994). The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13, 2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 3
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F. & Raina, S. (1995). Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14, 341 5-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 4
    • 0031048260 scopus 로고    scopus 로고
    • Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes
    • Fabianek, R.A., et al., & Thöny-Meyer, L. (1997). Characterization of the Bradyrhizobium japonicum CycY protein, a membrane-anchored periplasmic thioredoxin that may play a role as a reductant in the biogenesis of c-type cytochromes. J. Biol. Chem. 272, 4467-4473.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4467-4473
    • Fabianek, R.A.1    Thöny-Meyer, L.2
  • 6
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J.L., Bardwell, J.C.A. & Kuriyan, J. (1993). Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365, 464-468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3
  • 7
    • 0029973729 scopus 로고    scopus 로고
    • Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy
    • Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. & Creighton, T.E. (1996). Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35, 7684-7691.
    • (1996) Biochemistry , vol.35 , pp. 7684-7691
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 9
    • 0028225291 scopus 로고
    • Dissecting the mechanism of protein disulfide isomerase - Catalysis of disulfide bond formation in a model peptide
    • Darby, N.J., Freedman, R.B. & Creighton, T.E. (1994). Dissecting the mechanism of protein disulfide isomerase - catalysis of disulfide bond formation in a model peptide. Biochemistry 33, 7937-7947.
    • (1994) Biochemistry , vol.33 , pp. 7937-7947
    • Darby, N.J.1    Freedman, R.B.2    Creighton, T.E.3
  • 10
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. & Creighton, T.E. (1997). The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr. Biol. 7, 239-245.
    • (1997) Curr. Biol. , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 11
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M. & Glockshuber, R. (1993). Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci. 2, 717-726.
    • (1993) Protein Sci. , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 12
    • 0027254133 scopus 로고
    • The reactive and destabilising disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • Zapun, A., Bardwell, J.C.A. & Creighton, T.E. (1993). The reactive and destabilising disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32, 5083-5092.
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.A.2    Creighton, T.E.3
  • 13
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide isomerase from the equilibrium with glutathione and thioredoxin
    • Lundström, J. & Holmgren, A. (1993). Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry 32, 6649-6655.
    • (1993) Biochemistry , vol.32 , pp. 6649-6655
    • Lundström, J.1    Holmgren, A.2
  • 14
    • 0029590754 scopus 로고
    • Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase
    • Darby, N.J. & Creighton, T.E. (1995). Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34, 16770-16780.
    • (1995) Biochemistry , vol.34 , pp. 16770-16780
    • Darby, N.J.1    Creighton, T.E.2
  • 15
    • 0024324626 scopus 로고
    • Urea dependence of thiol-disulfide equilibria in thioredoxin: Confirmation of the linkage relationship and a sensitive assay for structure
    • Lin, T.-Y. & Kim, P.S. (1989). Urea dependence of thiol-disulfide equilibria in thioredoxin: confirmation of the linkage relationship and a sensitive assay for structure. Biochemistry 28, 5282-5287.
    • (1989) Biochemistry , vol.28 , pp. 5282-5287
    • Lin, T.-Y.1    Kim, P.S.2
  • 16
    • 0027358654 scopus 로고
    • The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form
    • Wunderlich, M., Jaenicke, R. & Glockshuber, R. (1993). The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form. J. mol. Biol. 233, 559-566.
    • (1993) J. Mol. Biol. , vol.233 , pp. 559-566
    • Wunderlich, M.1    Jaenicke, R.2    Glockshuber, R.3
  • 17
    • 0028360184 scopus 로고
    • Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Nelson, J.W. & Creighton, T.E. (1994). Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33, 5974-5983.
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 18
    • 0029559184 scopus 로고
    • Why is DsbA such an oxidizing disulfide catalyst?
    • Grauschopf, U., et al., & Bardwell, J.C.A. (1995). Why is DsbA such an oxidizing disulfide catalyst? Cell 83, 947-955.
    • (1995) Cell , vol.83 , pp. 947-955
    • Grauschopf, U.1    Bardwell, J.C.A.2
  • 19
    • 0030446158 scopus 로고    scopus 로고
    • Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase
    • Kortemme, T., Darby, N.J. & Creighton, T.E. (1996). Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Biochemistry 35, 14503-14511.
    • (1996) Biochemistry , vol.35 , pp. 14503-14511
    • Kortemme, T.1    Darby, N.J.2    Creighton, T.E.3
  • 20
    • 0031010755 scopus 로고    scopus 로고
    • The uncharged surface features surrounding the active-site of E. coli DsbA are conserved and are implicated in peptide binding
    • Guddat, LW., Bardwell, J.C.A., Zander, T. & Martin, J.L (1997). The uncharged surface features surrounding the active-site of E. coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 6, 1148-1156.
    • (1997) Protein Sci. , vol.6 , pp. 1148-1156
    • Guddat, L.W.1    Bardwell, J.C.A.2    Zander, T.3    Martin, J.L.4
  • 21
    • 0030880594 scopus 로고    scopus 로고
    • Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability
    • Guddat, L.W., et al., & Martin, J.L. (1997). Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6, 1893-1900.
    • (1997) Protein Sci. , vol.6 , pp. 1893-1900
    • Guddat, L.W.1    Martin, J.L.2
  • 22
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W. & Schulten, K. (1997). Protein domain movements: detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins 29, 1-14.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 23
    • 0028774178 scopus 로고
    • High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin
    • Jeng, M.-F., et al., & Dyson, H.J. (1994). High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2, 853-868.
    • (1994) Structure , vol.2 , pp. 853-868
    • Jeng, M.-F.1    Dyson, H.J.2
  • 24
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin, J., Clore, G.M. & Gronenborn, A.M. (1994). The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2, 503-522.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 25
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structure of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • Weichsel, A., Gasdaska, J.R., Powis, G. & Montfort, W.R. (1996). Crystal structure of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 4, 735-751.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 26
    • 0017411710 scopus 로고
    • The protein data bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The protein data bank: a computer-based archival file for macromolecular structures. J. mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 27
    • 0029159834 scopus 로고
    • The structure of a reduced mutant T4 glutaredoxin
    • Ingelman, M., Nordlund, P. & Eklund, H. (1995). The structure of a reduced mutant T4 glutaredoxin. FEBS Lett. 370, 209-211.
    • (1995) FEBS Lett. , vol.370 , pp. 209-211
    • Ingelman, M.1    Nordlund, P.2    Eklund, H.3
  • 28
    • 0027291239 scopus 로고
    • Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
    • Missiakas, D., Georgopoulos, C. & Raina, S. (1993). Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl Acad. Sci. USA 90, 7084-7088.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7084-7088
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 29
    • 0001473631 scopus 로고
    • A neutron diffraction study of L-cysteine
    • Kerr, K.A., Ashmore, J.P. & Koetzle, T.F. (1975). A neutron diffraction study of L-cysteine. Acta Crystallogr. B31, 2022 - 2026.
    • (1975) Acta Crystallogr. , vol.B31 , pp. 2022-2026
    • Kerr, K.A.1    Ashmore, J.P.2    Koetzle, T.F.3
  • 30
    • 0001282755 scopus 로고
    • NH...S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein
    • Adman, E., Watenpaugh, K.D. & Jensen, L.H. (1975). NH...S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. Proc. Natl Acad. Sci. USA 72, 4854-4858.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 4854-4858
    • Adman, E.1    Watenpaugh, K.D.2    Jensen, L.H.3
  • 32
    • 0021745755 scopus 로고
    • Functional group contributions to drug-receptor interactions
    • Andrews, P.R., Craik, D.J. & Martin, J.L. (1984). Functional group contributions to drug-receptor interactions. J. Med. Chem. 27, 1648-1657.
    • (1984) J. Med. Chem. , vol.27 , pp. 1648-1657
    • Andrews, P.R.1    Craik, D.J.2    Martin, J.L.3
  • 33
    • 0021828928 scopus 로고
    • Hydrogen bonding and biological specificity analysed by protein engineering
    • Fersht, A.R., et al., & Winter, G. (1987). Hydrogen bonding and biological specificity analysed by protein engineering. Nature 314, 235-238.
    • (1987) Nature , vol.314 , pp. 235-238
    • Fersht, A.R.1    Winter, G.2
  • 34
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • Hol, W.G. (1985). The role of the α-helix dipole in protein function and structure. Prog. Biophys. mol. Biol. 45, 149-195.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.1
  • 35
    • 0028886558 scopus 로고
    • a values in proteins of the thioredoxin family
    • a values in proteins of the thioredoxin family. J. mol. Biol. 253, 799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 36
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis, G.-B. & Holmgren, A. (1980). Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255, 10261-10265.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10261-10265
    • Kallis, G.-B.1    Holmgren, A.2
  • 37
    • 0025755942 scopus 로고
    • Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR
    • Dyson, H.J., Tennant, L.L. & Holmgren, A. (1991). Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR. Biochemistry 30, 4262-4268.
    • (1991) Biochemistry , vol.30 , pp. 4262-4268
    • Dyson, H.J.1    Tennant, L.L.2    Holmgren, A.3
  • 38
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin: Characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR
    • Forman-Kay, J.D., Clore, G.M. & Gronenborn, A.M. (1992). Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR. Biochemistry 31, 3442-3452.
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 39
    • 0025124855 scopus 로고
    • Yeast thioltransferase - The active site cysteines display differential reactivity
    • Gan, Z.-R., Sardana, M.K., Jacobs, J.W. & Polokoff, M.A. (1990). Yeast thioltransferase - the active site cysteines display differential reactivity. Arch. Biochem. Biophys. 282, 110-115.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 110-115
    • Gan, Z.-R.1    Sardana, M.K.2    Jacobs, J.W.3    Polokoff, M.A.4
  • 40
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal, J.J., Starke, D.W., Gravina, S.A. & Hocevar, B.A. (1991). Thioltransferase in human red blood cells: kinetics and equilibrium. Biochemistry 30, 8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 41
    • 0025788552 scopus 로고
    • Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis
    • Yang, Y. & Wells, W.W. (1991). Identification and characterization of the functional amino acids at the active center of pig liver thioltransferase by site-directed mutagenesis. J. Biol. Chem. 266, 12759-12765.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2
  • 42
    • 0032485920 scopus 로고    scopus 로고
    • Structure of reduced DsbA from Escherichia coli in solution
    • Schirra, H.J., et al., & Glockshuber, R. (1998). Structure of reduced DsbA from Escherichia coli in solution. Biochemistry 37, 6263-6276.
    • (1998) Biochemistry , vol.37 , pp. 6263-6276
    • Schirra, H.J.1    Glockshuber, R.2
  • 43
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C.A., McGovern, K. & Beckwith, J. (1991). Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 44
    • 0027223571 scopus 로고
    • Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo
    • Martin, J.L., Waksman, G., Bardwell, J.C.A., Beckwith, J. & Kuriyan, J. (1993). Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J. mol. Biol. 230, 1097-1100.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1097-1100
    • Martin, J.L.1    Waksman, G.2    Bardwell, J.C.A.3    Beckwith, J.4    Kuriyan, J.5
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. (1996). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1996) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brünger, AT. (1990). Extension of molecular replacement: a new search strategy based on Patterson correlation refinement. Acta Crystallogr. A46, 46-57.
    • (1990) Acta Crystallogr. , vol.A46 , pp. 46-57
    • Brünger, A.T.1
  • 48
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, AT. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 49
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • Kleywegt, G.J. & Brünger, AT. (1996). Checking your imagination: applications of the free R value. Structure 4, 897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 50
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 51
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 52
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 53
    • 0000913086 scopus 로고
    • A fast algorithm for rendering spacefilling molecular pictures
    • Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering spacefilling molecular pictures. J. mol. Graphics 6, 219-222.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-222
    • Bacon, D.J.1    Anderson, W.F.2
  • 54
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 55
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. mol. Graphics 11, 134-138.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1


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