메뉴 건너뛰기




Volumn 397, Issue 5, 2010, Pages 1316-1328

Molecular structure of the n-terminal domain of the APC/C subunit Cdc27 reveals a homo-dimeric tetratricopeptide repeat architecture

Author keywords

APC C; Cdc27; Cell cycle; Crystal structure; Tetratricopeptide repeat TPR

Indexed keywords

ANAPHASE PROMOTING COMPLEX; CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 27; TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 77950489085     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.045     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: it's not just for mitosis any more
    • Harper J.W., Burton J.L., Solomon M.J. The anaphase-promoting complex: it's not just for mitosis any more. Genes Dev. 2002, 16:2179-2206.
    • (2002) Genes Dev. , vol.16 , pp. 2179-2206
    • Harper, J.W.1    Burton, J.L.2    Solomon, M.J.3
  • 2
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: a machine designed to destroy
    • Peters J.M. The anaphase promoting complex/cyclosome: a machine designed to destroy. Nat. Rev. Mol. Cell Biol. 2006, 7:644-656.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 3
    • 33751213571 scopus 로고    scopus 로고
    • Precise destruction: an emerging picture of the APC
    • Thornton B.R., Toczyski D.P. Precise destruction: an emerging picture of the APC. Genes Dev. 2006, 20:3069-3078.
    • (2006) Genes Dev. , vol.20 , pp. 3069-3078
    • Thornton, B.R.1    Toczyski, D.P.2
  • 4
    • 30444449969 scopus 로고    scopus 로고
    • Mitosis: a matter of getting rid of the right protein at the right time
    • Pines J. Mitosis: a matter of getting rid of the right protein at the right time. Trends Cell Biol. 2006, 16:55-63.
    • (2006) Trends Cell Biol. , vol.16 , pp. 55-63
    • Pines, J.1
  • 8
    • 0036289141 scopus 로고    scopus 로고
    • Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit
    • Au S.W., Leng X., Harper J.W., Barford D. Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. J. Mol. Biol. 2002, 316:955-968.
    • (2002) J. Mol. Biol. , vol.316 , pp. 955-968
    • Au, S.W.1    Leng, X.2    Harper, J.W.3    Barford, D.4
  • 9
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P., et al. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 2002, 416:703-709.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1    Schulman, B.A.2    Song, L.3    Miller, J.J.4    Jeffrey, P.D.5    Wang, P.6
  • 10
    • 67649306803 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7
    • Han D., Kim K., Kim Y., Kang Y., Lee J.Y., Kim Y. Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7. J. Biol. Chem. 2009, 284:15137-15146.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15137-15146
    • Han, D.1    Kim, K.2    Kim, Y.3    Kang, Y.4    Lee, J.Y.5    Kim, Y.6
  • 11
    • 69949190148 scopus 로고    scopus 로고
    • Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure
    • Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A. Insights into anaphase promoting complex TPR subdomain assembly from a CDC26-APC6 structure. Nat. Struct. Mol. Biol. 2009, 16:987-989.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 987-989
    • Wang, J.1    Dye, B.T.2    Rajashankar, K.R.3    Kurinov, I.4    Schulman, B.A.5
  • 12
    • 29144527503 scopus 로고    scopus 로고
    • Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C
    • Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Muller S.A., et al. Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C. Mol. Cell 2005, 20:867-879.
    • (2005) Mol. Cell , vol.20 , pp. 867-879
    • Dube, P.1    Herzog, F.2    Gieffers, C.3    Sander, B.4    Riedel, D.5    Muller, S.A.6
  • 13
    • 29144484041 scopus 로고    scopus 로고
    • Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation
    • Passmore L.A., Booth C.R., Venien-Bryan C., Ludtke S.J., Fioretto C., Johnson L.N., et al. Structural analysis of the anaphase-promoting complex reveals multiple active sites and insights into polyubiquitylation. Mol Cell 2005, 20:855-866.
    • (2005) Mol Cell , vol.20 , pp. 855-866
    • Passmore, L.A.1    Booth, C.R.2    Venien-Bryan, C.3    Ludtke, S.J.4    Fioretto, C.5    Johnson, L.N.6
  • 14
    • 36749061942 scopus 로고    scopus 로고
    • Structural organization of the anaphase-promoting complex bound to the mitotic activator Slp1
    • Ohi M.D., Feoktistova A., Ren L., Yip C., Cheng Y., Chen J.S., et al. Structural organization of the anaphase-promoting complex bound to the mitotic activator Slp1. Mol. Cell 2007, 28:871-885.
    • (2007) Mol. Cell , vol.28 , pp. 871-885
    • Ohi, M.D.1    Feoktistova, A.2    Ren, L.3    Yip, C.4    Cheng, Y.5    Chen, J.S.6
  • 15
    • 62449220573 scopus 로고    scopus 로고
    • Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex
    • Herzog F., Primorac I., Dube P., Lenart P., Sander B., Mechtler K., et al. Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex. Science 2009, 323:1477-1481.
    • (2009) Science , vol.323 , pp. 1477-1481
    • Herzog, F.1    Primorac, I.2    Dube, P.3    Lenart, P.4    Sander, B.5    Mechtler, K.6
  • 16
    • 0343829343 scopus 로고    scopus 로고
    • Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae
    • Zachariae W., Shin T.H., Galova M., Obermaier B., Nasmyth K. Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae. Science 1996, 274:1201-1204.
    • (1996) Science , vol.274 , pp. 1201-1204
    • Zachariae, W.1    Shin, T.H.2    Galova, M.3    Obermaier, B.4    Nasmyth, K.5
  • 17
    • 0029909251 scopus 로고    scopus 로고
    • Identification of BIME as a subunit of the anaphase-promoting complex
    • Peters J.M., King R.W., Hoog C., Kirschner M.W. Identification of BIME as a subunit of the anaphase-promoting complex. Science 1996, 274:1199-1201.
    • (1996) Science , vol.274 , pp. 1199-1201
    • Peters, J.M.1    King, R.W.2    Hoog, C.3    Kirschner, M.W.4
  • 18
    • 0032518686 scopus 로고    scopus 로고
    • Budding yeast RSI1/APC2, a novel gene necessary for initiation of anaphase, encodes an APC subunit
    • Kramer K.M., Fesquet D., Johnson A.L., Johnston L.H. Budding yeast RSI1/APC2, a novel gene necessary for initiation of anaphase, encodes an APC subunit. EMBO J. 1998, 17:498-506.
    • (1998) EMBO J. , vol.17 , pp. 498-506
    • Kramer, K.M.1    Fesquet, D.2    Johnson, A.L.3    Johnston, L.H.4
  • 19
    • 0032549116 scopus 로고    scopus 로고
    • Identification of a cullin homology region in a subunit of the anaphase-promoting complex
    • Yu H., Peters J.M., King R.W., Page A.M., Hieter P., Kirschner M.W. Identification of a cullin homology region in a subunit of the anaphase-promoting complex. Science 1998, 279:1219-1222.
    • (1998) Science , vol.279 , pp. 1219-1222
    • Yu, H.1    Peters, J.M.2    King, R.W.3    Page, A.M.4    Hieter, P.5    Kirschner, M.W.6
  • 20
    • 0032549115 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins
    • Zachariae W., Shevchenko A., Andrews P.D., Ciosk R., Galova M., Stark M.J., et al. Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins. Science 1998, 279:1216-1219.
    • (1998) Science , vol.279 , pp. 1216-1219
    • Zachariae, W.1    Shevchenko, A.2    Andrews, P.D.3    Ciosk, R.4    Galova, M.5    Stark, M.J.6
  • 21
    • 0036900585 scopus 로고    scopus 로고
    • Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes
    • Yoon H.J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J., Gould K.L. Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes. Curr. Biol. 2002, 12:2048-2054.
    • (2002) Curr. Biol. , vol.12 , pp. 2048-2054
    • Yoon, H.J.1    Feoktistova, A.2    Wolfe, B.A.3    Jennings, J.L.4    Link, A.J.5    Gould, K.L.6
  • 22
    • 0037450770 scopus 로고    scopus 로고
    • Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition
    • Passmore L.A., McCormack E.A., Au S.W., Paul A., Willison K.R., Harper J.W., Barford D. Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J. 2003, 22:786-796.
    • (2003) EMBO J. , vol.22 , pp. 786-796
    • Passmore, L.A.1    McCormack, E.A.2    Au, S.W.3    Paul, A.4    Willison, K.R.5    Harper, J.W.6    Barford, D.7
  • 23
    • 1842609712 scopus 로고    scopus 로고
    • Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-promoting complex stabilizing the association of Cdc16 and Cdc27
    • Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A., Oelschlaegel T., et al. Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-promoting complex stabilizing the association of Cdc16 and Cdc27. Mol. Cell. Biol. 2004, 24:3562-3576.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3562-3576
    • Schwickart, M.1    Havlis, J.2    Habermann, B.3    Bogdanova, A.4    Camasses, A.5    Oelschlaegel, T.6
  • 24
    • 0034255264 scopus 로고    scopus 로고
    • The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex
    • Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.M. The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proc. Natl Acad. Sci. USA 2000, 97:8973-8978.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8973-8978
    • Gmachl, M.1    Gieffers, C.2    Podtelejnikov, A.V.3    Mann, M.4    Peters, J.M.5
  • 26
    • 0035661566 scopus 로고    scopus 로고
    • APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex
    • Tang Z., Li B., Bharadwaj R., Zhu H., Ozkan E., Hakala K., Deisenhofer J., Yu H. APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol. Biol. Cell 2001, 12:3839-3851.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Li, B.2    Bharadwaj, R.3    Zhu, H.4    Ozkan, E.5    Hakala, K.6    Deisenhofer, J.7    Yu, H.8
  • 27
    • 0030926522 scopus 로고    scopus 로고
    • A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (anaphase-promoting complex)
    • Lupas A., Baumeister W., Hofmann K. A repetitive sequence in subunits of the 26S proteasome and 20S cyclosome (anaphase-promoting complex). Trends Biochem. Sci. 1997, 22:195-196.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 195-196
    • Lupas, A.1    Baumeister, W.2    Hofmann, K.3
  • 29
    • 0042921286 scopus 로고    scopus 로고
    • TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1
    • Vodermaier H.C., Gieffers C., Maurer-Stroh S., Eisenhaber F., Peters J.M. TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1. Curr. Biol. 2003, 13:1459-1468.
    • (2003) Curr. Biol. , vol.13 , pp. 1459-1468
    • Vodermaier, H.C.1    Gieffers, C.2    Maurer-Stroh, S.3    Eisenhaber, F.4    Peters, J.M.5
  • 30
    • 0028168867 scopus 로고
    • Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis
    • Lamb J.R., Michaud W.A., Sikorski R.S., Hieter P.A. Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis. EMBO J. 1994, 13:4321-4328.
    • (1994) EMBO J. , vol.13 , pp. 4321-4328
    • Lamb, J.R.1    Michaud, W.A.2    Sikorski, R.S.3    Hieter, P.A.4
  • 31
    • 0035903652 scopus 로고    scopus 로고
    • Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC
    • Schwab M., Neutzner M., Mocker D., Seufert W. Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC. EMBO J. 2001, 20:5165-5175.
    • (2001) EMBO J. , vol.20 , pp. 5165-5175
    • Schwab, M.1    Neutzner, M.2    Mocker, D.3    Seufert, W.4
  • 32
    • 19444378969 scopus 로고    scopus 로고
    • The WD40 propeller domain of Cdh1 functions as a destruction box receptor for APC/C substrates
    • Kraft C., Vodermaier H.C., Maurer-Stroh S., Eisenhaber F., Peters J.M. The WD40 propeller domain of Cdh1 functions as a destruction box receptor for APC/C substrates. Mol. Cell 2005, 18:543-553.
    • (2005) Mol. Cell , vol.18 , pp. 543-553
    • Kraft, C.1    Vodermaier, H.C.2    Maurer-Stroh, S.3    Eisenhaber, F.4    Peters, J.M.5
  • 33
    • 63649134628 scopus 로고    scopus 로고
    • Analysis of activator-binding sites on the APC/C supports a cooperative substrate-binding mechanism
    • Matyskiela M.E., Morgan D.O. Analysis of activator-binding sites on the APC/C supports a cooperative substrate-binding mechanism. Mol. Cell 2009, 34:68-80.
    • (2009) Mol. Cell , vol.34 , pp. 68-80
    • Matyskiela, M.E.1    Morgan, D.O.2
  • 34
    • 33744813542 scopus 로고    scopus 로고
    • Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C
    • Hayes M.J., Kimata Y., Wattam S.L., Lindon C., Mao G., Yamano H., Fry A.M. Early mitotic degradation of Nek2A depends on Cdc20-independent interaction with the APC/C. Nat. Cell Biol. 2006, 8:607-614.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 607-614
    • Hayes, M.J.1    Kimata, Y.2    Wattam, S.L.3    Lindon, C.4    Mao, G.5    Yamano, H.6    Fry, A.M.7
  • 35
    • 0037126610 scopus 로고    scopus 로고
    • APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box
    • Hames R.S., Wattam S.L., Yamano H., Bacchieri R., Fry A.M. APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box. EMBO J. 2001, 20:7117-7127.
    • (2001) EMBO J. , vol.20 , pp. 7117-7127
    • Hames, R.S.1    Wattam, S.L.2    Yamano, H.3    Bacchieri, R.4    Fry, A.M.5
  • 36
    • 0035936144 scopus 로고    scopus 로고
    • Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi
    • Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., et al. Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi. Nature 2001, 414:450-453.
    • (2001) Nature , vol.414 , pp. 450-453
    • Katinka, M.D.1    Duprat, S.2    Cornillot, E.3    Metenier, G.4    Thomarat, F.5    Prensier, G.6
  • 38
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • Main E.R., Xiong Y., Cocco M.J., D'Andrea L., Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure 2003, 11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 39
    • 77950496292 scopus 로고    scopus 로고
    • Crystal structure of an 8 repeat consensus TPR superhelix (trigonal crystal form)
    • Kajander, T., Lopez-Cortajarena, A., Mochrie, S. & Regan, L. (2006). Crystal structure of an 8 repeat consensus TPR superhelix (trigonal crystal form).
    • (2006)
    • Kajander, T.1    Lopez-Cortajarena, A.2    Mochrie, S.3    Regan, L.4
  • 40
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions
    • Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 1998, 17:1192-1199.
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 41
    • 0025034814 scopus 로고
    • Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+
    • Hirano T., Kinoshita N., Morikawa K., Yanagida M. Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+. Cell 1990, 60:319-328.
    • (1990) Cell , vol.60 , pp. 319-328
    • Hirano, T.1    Kinoshita, N.2    Morikawa, K.3    Yanagida, M.4
  • 42
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski R.S., Boguski M.S., Goebl M., Hieter P. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 1990, 60:307-317.
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 43
  • 45
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000, 101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6
  • 46
    • 0033664345 scopus 로고    scopus 로고
    • Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5
    • Gatto G.J., Geisbrecht B.V., Gould S.J., Berg J.M. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat. Struct. Biol. 2000, 7:1091-1095.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1091-1095
    • Gatto, G.J.1    Geisbrecht, B.V.2    Gould, S.J.3    Berg, J.M.4
  • 47
    • 0025871806 scopus 로고
    • BimA encodes a member of the tetratricopeptide repeat family of proteins and is required for the completion of mitosis in Aspergillus nidulans
    • O'Donnell K.L., Osmani A.H., Osmani S.A., Morris N.R. bimA encodes a member of the tetratricopeptide repeat family of proteins and is required for the completion of mitosis in Aspergillus nidulans. J. Cell. Sci. 1991, 99:711-719.
    • (1991) J. Cell. Sci. , vol.99 , pp. 711-719
    • O'Donnell, K.L.1    Osmani, A.H.2    Osmani, S.A.3    Morris, N.R.4
  • 49
    • 13244298548 scopus 로고    scopus 로고
    • APC activators caught by their tails?
    • Vodermaier H.C., Peters J.M. APC activators caught by their tails?. Cell Cycle 2004, 3:265-266.
    • (2004) Cell Cycle , vol.3 , pp. 265-266
    • Vodermaier, H.C.1    Peters, J.M.2
  • 50
    • 55949119059 scopus 로고    scopus 로고
    • A role for the Fizzy/Cdc20 family of proteins in activation of the APC/C distinct from substrate recruitment
    • Kimata Y., Baxter J.E., Fry A.M., Yamano H. A role for the Fizzy/Cdc20 family of proteins in activation of the APC/C distinct from substrate recruitment. Mol. Cell 2008, 32:576-583.
    • (2008) Mol. Cell , vol.32 , pp. 576-583
    • Kimata, Y.1    Baxter, J.E.2    Fry, A.M.3    Yamano, H.4
  • 51
    • 0027412196 scopus 로고
    • ALSCRIPT: a tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 1993, 6:37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 54
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.