메뉴 건너뛰기




Volumn 386, Issue 1, 2009, Pages 121-133

Crystal Structure of the Parasporin-2 Bacillus thuringiensis Toxin That Recognizes Cancer Cells

Author keywords

Bacillus thuringiensis; Cry protein; parasporin; pore forming toxin; transmembrane hairpin

Indexed keywords

AEROLYSIN; BACILLUS THURINGIENSIS TOXIN; PARASPORIN 2; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 58549090523     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.12.002     Document Type: Article
Times cited : (82)

References (66)
  • 1
    • 0032996801 scopus 로고    scopus 로고
    • Bacillus thuringiensis toxin-mediated insect resistance in plants
    • de Maagd R.A., Bosch D., and Stiekema W. Bacillus thuringiensis toxin-mediated insect resistance in plants. Trends Plant Sci. 4 (1999) 9-13
    • (1999) Trends Plant Sci. , vol.4 , pp. 9-13
    • de Maagd, R.A.1    Bosch, D.2    Stiekema, W.3
  • 4
    • 0348047325 scopus 로고    scopus 로고
    • Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria
    • de Maagd R.A., Bravo A., Berry C., Crickmore N., and Schnepf H.E. Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria. Annu. Rev. Genet. 37 (2003) 409-433
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 409-433
    • de Maagd, R.A.1    Bravo, A.2    Berry, C.3    Crickmore, N.4    Schnepf, H.E.5
  • 5
    • 0035313205 scopus 로고    scopus 로고
    • How Bacillus thuringiensis has evolved specific toxins to colonize the insect world
    • de Maagd R.A., Bravo A., and Crickmore N. How Bacillus thuringiensis has evolved specific toxins to colonize the insect world. Trends Genet. 17 (2001) 193-199
    • (2001) Trends Genet. , vol.17 , pp. 193-199
    • de Maagd, R.A.1    Bravo, A.2    Crickmore, N.3
  • 6
    • 0034859678 scopus 로고    scopus 로고
    • Structural implications for the transformation of the Bacillus thuringiensis delta-endotoxins from water-soluble to membrane-inserted forms
    • Li J., Derbyshire D.J., Promdonkoy B., and Ellar D.J. Structural implications for the transformation of the Bacillus thuringiensis delta-endotoxins from water-soluble to membrane-inserted forms. Biochem. Soc. Trans. 29 (2001) 571-577
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 571-577
    • Li, J.1    Derbyshire, D.J.2    Promdonkoy, B.3    Ellar, D.J.4
  • 7
    • 0022641395 scopus 로고
    • Insect toxicity of Bacillus thuringiensis isolated from soils of Japan
    • Ohba M., and Aizawa K. Insect toxicity of Bacillus thuringiensis isolated from soils of Japan. J. Invertebr. Pathol. 47 (1986) 12-20
    • (1986) J. Invertebr. Pathol. , vol.47 , pp. 12-20
    • Ohba, M.1    Aizawa, K.2
  • 8
    • 0026596692 scopus 로고
    • Distribution, frequency, and diversity of Bacillus thuringiensis in an animal feed mill
    • Meadows M.P., Ellis D.J., Butt J., Jarrett P., and Burges H.D. Distribution, frequency, and diversity of Bacillus thuringiensis in an animal feed mill. Appl. Environ. Microbiol. 58 (1992) 1344-1350
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1344-1350
    • Meadows, M.P.1    Ellis, D.J.2    Butt, J.3    Jarrett, P.4    Burges, H.D.5
  • 9
    • 0033032037 scopus 로고    scopus 로고
    • Unique activity associated with non-insecticidal Bacillus thuringiensis parasporal inclusions: in vitro cell-killing action on human cancer cells
    • Mizuki E., Ohba M., Akao T., Yamashita S., Saitoh H., and Park Y.S. Unique activity associated with non-insecticidal Bacillus thuringiensis parasporal inclusions: in vitro cell-killing action on human cancer cells. J. Appl. Microbiol. 86 (1999) 477-486
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 477-486
    • Mizuki, E.1    Ohba, M.2    Akao, T.3    Yamashita, S.4    Saitoh, H.5    Park, Y.S.6
  • 11
    • 17044401845 scopus 로고    scopus 로고
    • Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis
    • Katayama H., Yokota H., Akao T., Nakamura O., Ohba M., Mekada E., and Mizuki E. Parasporin-1, a novel cytotoxic protein to human cells from non-insecticidal parasporal inclusions of Bacillus thuringiensis. J. Biochem. 137 (2005) 17-25
    • (2005) J. Biochem. , vol.137 , pp. 17-25
    • Katayama, H.1    Yokota, H.2    Akao, T.3    Nakamura, O.4    Ohba, M.5    Mekada, E.6    Mizuki, E.7
  • 12
    • 2442675505 scopus 로고    scopus 로고
    • A Bacillus thuringiensis crystal protein with selective cytocidal action to human cells
    • Ito A., Sasaguri Y., Kitada S., Kusaka Y., Kuwano K., Masutomi K., et al. A Bacillus thuringiensis crystal protein with selective cytocidal action to human cells. J. Biol. Chem. 279 (2004) 21282-21286
    • (2004) J. Biol. Chem. , vol.279 , pp. 21282-21286
    • Ito, A.1    Sasaguri, Y.2    Kitada, S.3    Kusaka, Y.4    Kuwano, K.5    Masutomi, K.6
  • 13
    • 0033781415 scopus 로고    scopus 로고
    • Characterization of the anti-cancer-cell parasporal proteins of a Bacillus thuringiensis isolate
    • Yamashita S., Akao T., Mizuki E., Saitoh H., Higuchi K., Park Y.S., et al. Characterization of the anti-cancer-cell parasporal proteins of a Bacillus thuringiensis isolate. Can. J. Microbiol. 46 (2000) 913-919
    • (2000) Can. J. Microbiol. , vol.46 , pp. 913-919
    • Yamashita, S.1    Akao, T.2    Mizuki, E.3    Saitoh, H.4    Higuchi, K.5    Park, Y.S.6
  • 14
    • 0034720456 scopus 로고    scopus 로고
    • Noninsecticidal parasporal proteins of a Bacillus thuringiensis serovar shandongiensis isolate exhibit a preferential cytotoxicity against human leukemic T cells
    • Lee D.W., Akao T., Yamashita S., Katayama H., Maeda M., Saitoh H., et al. Noninsecticidal parasporal proteins of a Bacillus thuringiensis serovar shandongiensis isolate exhibit a preferential cytotoxicity against human leukemic T cells. Biochem. Biophys. Res. Commun. 272 (2000) 218-223
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 218-223
    • Lee, D.W.1    Akao, T.2    Yamashita, S.3    Katayama, H.4    Maeda, M.5    Saitoh, H.6
  • 15
    • 0033853434 scopus 로고    scopus 로고
    • In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells
    • Kim H.S., Yamashita S., Akao T., Saitoh H., Higuchi K., Park Y.S., et al. In vitro cytotoxicity of non-Cyt inclusion proteins of a Bacillus thuringiensis isolate against human cells, including cancer cells. J. Appl. Microbiol. 89 (2000) 16-23
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 16-23
    • Kim, H.S.1    Yamashita, S.2    Akao, T.3    Saitoh, H.4    Higuchi, K.5    Park, Y.S.6
  • 16
    • 33748742185 scopus 로고    scopus 로고
    • Cytocidal actions of parasporin-2, an anti-tumor crystal toxin from Bacillus thuringiensis
    • Kitada S., Abe Y., Shimada H., Kusaka Y., Matsuo Y., Katayama H., et al. Cytocidal actions of parasporin-2, an anti-tumor crystal toxin from Bacillus thuringiensis. J. Biol. Chem. 281 (2006) 26350-26360
    • (2006) J. Biol. Chem. , vol.281 , pp. 26350-26360
    • Kitada, S.1    Abe, Y.2    Shimada, H.3    Kusaka, Y.4    Matsuo, Y.5    Katayama, H.6
  • 18
  • 19
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 21
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • Morse R.J., Yamamoto T., and Stroud R.M. Structure of Cry2Aa suggests an unexpected receptor binding epitope. Structure 9 (2001) 409-417
    • (2001) Structure , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 22
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • Li J., Carroll J., and Ellar D.J. Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution. Nature 353 (1991) 815-821
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 24
    • 33646257356 scopus 로고    scopus 로고
    • Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Angstrom resolution
    • Boonserm P., Mo M., Angsuthanasombat C., and Lescar J. Structure of the functional form of the mosquito larvicidal Cry4Aa toxin from Bacillus thuringiensis at a 2.8-Angstrom resolution. J. Bacteriol. 188 (2006) 3391-3401
    • (2006) J. Bacteriol. , vol.188 , pp. 3391-3401
    • Boonserm, P.1    Mo, M.2    Angsuthanasombat, C.3    Lescar, J.4
  • 25
    • 16244392435 scopus 로고    scopus 로고
    • Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications
    • Boonserm P., Davis P., Ellar D.J., and Li J. Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications. J. Mol. Biol. 348 (2005) 363-382
    • (2005) J. Mol. Biol. , vol.348 , pp. 363-382
    • Boonserm, P.1    Davis, P.2    Ellar, D.J.3    Li, J.4
  • 26
    • 0029669956 scopus 로고    scopus 로고
    • Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation
    • Li J., Koni P.A., and Ellar D.J. Structure of the mosquitocidal δ-endotoxin CytB from Bacillus thuringiensis sp. kyushuensis and implications for membrane pore formation. J. Mol. Biol. 257 (1996) 129-152
    • (1996) J. Mol. Biol. , vol.257 , pp. 129-152
    • Li, J.1    Koni, P.A.2    Ellar, D.J.3
  • 27
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm L., Kaariainen S., Rosenstrom P., and Schenkel A. Searching protein structure databases with DaliLite v.3. Bioinformatics 24 (2008) 2780-2781
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 28
    • 33645032104 scopus 로고    scopus 로고
    • Nontoxic crystal protein from Bacillus thuringiensis demonstrates a remarkable structural similarity to beta-pore-forming toxins
    • Akiba T., Higuchi K., Mizuki E., Ekino K., Shin T., Ohba M., et al. Nontoxic crystal protein from Bacillus thuringiensis demonstrates a remarkable structural similarity to beta-pore-forming toxins. Proteins 63 (2006) 243-248
    • (2006) Proteins , vol.63 , pp. 243-248
    • Akiba, T.1    Higuchi, K.2    Mizuki, E.3    Ekino, K.4    Shin, T.5    Ohba, M.6
  • 29
    • 3542993232 scopus 로고    scopus 로고
    • Clostridium perfringens e{open}-toxin shows structural similarity to the pore-forming toxin aerolysin
    • Cole A.R., Gibert M., Popoff M., Moss D.S., Titball R.W., and Basak A.K. Clostridium perfringens e{open}-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat. Struct. Biol. 11 (2004) 797-798
    • (2004) Nat. Struct. Biol. , vol.11 , pp. 797-798
    • Cole, A.R.1    Gibert, M.2    Popoff, M.3    Moss, D.S.4    Titball, R.W.5    Basak, A.K.6
  • 31
    • 20444471526 scopus 로고    scopus 로고
    • Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars
    • Mancheno J.M., Tateno H., Goldstein I.J., Martinez-Ripoll M., and Hermoso J.A. Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars. J. Biol. Chem. 280 (2005) 17251-17259
    • (2005) J. Biol. Chem. , vol.280 , pp. 17251-17259
    • Mancheno, J.M.1    Tateno, H.2    Goldstein, I.J.3    Martinez-Ripoll, M.4    Hermoso, J.A.5
  • 32
    • 39049099938 scopus 로고    scopus 로고
    • Raft-targeting and oligomerization of parasporin-2, a Bacillus thuringiensis crystal protein with anti-tumour activity
    • Abe Y., Shimada H., and Kitada S. Raft-targeting and oligomerization of parasporin-2, a Bacillus thuringiensis crystal protein with anti-tumour activity. J. Biochem. 143 (2008) 269-275
    • (2008) J. Biochem. , vol.143 , pp. 269-275
    • Abe, Y.1    Shimada, H.2    Kitada, S.3
  • 33
    • 0042666840 scopus 로고    scopus 로고
    • Hydralysin, a novel animal group-selective paralytic and cytolytic protein from a noncnidocystic origin in hydra
    • Zhang M., Fishman Y., Sher D., and Zlotkin E. Hydralysin, a novel animal group-selective paralytic and cytolytic protein from a noncnidocystic origin in hydra. Biochemistry 42 (2003) 8939-8944
    • (2003) Biochemistry , vol.42 , pp. 8939-8944
    • Zhang, M.1    Fishman, Y.2    Sher, D.3    Zlotkin, E.4
  • 35
    • 23844486577 scopus 로고    scopus 로고
    • Identification of a novel cytotoxic protein, Cry45Aa, from Bacillus thuringiensis A1470 and its selective cytotoxic activity against various mammalian cell lines
    • Okumura S., Saitoh H., Ishikawa T., Wasano N., Yamashita S., Kusumoto K., et al. Identification of a novel cytotoxic protein, Cry45Aa, from Bacillus thuringiensis A1470 and its selective cytotoxic activity against various mammalian cell lines. J. Agric. Food Chem. 53 (2005) 6313-6318
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 6313-6318
    • Okumura, S.1    Saitoh, H.2    Ishikawa, T.3    Wasano, N.4    Yamashita, S.5    Kusumoto, K.6
  • 36
    • 0142103664 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins
    • Tateno H., and Goldstein I.J. Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins. J. Biol. Chem. 278 (2003) 40455-40463
    • (2003) J. Biol. Chem. , vol.278 , pp. 40455-40463
    • Tateno, H.1    Goldstein, I.J.2
  • 38
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., and Gouaux J.E. Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274 (1996) 1859-1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 39
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson R., Nariya H., Yokota K., Kamio Y., and Gouaux E. Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6 (1999) 134-140
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 40
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3 (1996) 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 41
    • 0031936213 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin
    • Diep D.B., Nelson K.L., Raja S.M., Pleshak E.N., and Buckley J.T. Glycosylphosphatidylinositol anchors of membrane glycoproteins are binding determinants for the channel-forming toxin aerolysin. J. Biol. Chem. 273 (1998) 2355-2360
    • (1998) J. Biol. Chem. , vol.273 , pp. 2355-2360
    • Diep, D.B.1    Nelson, K.L.2    Raja, S.M.3    Pleshak, E.N.4    Buckley, J.T.5
  • 42
    • 0034176550 scopus 로고    scopus 로고
    • Adventures of a pore-forming toxin at the target cell surface
    • Abrami L., Fivaz M., and van der Goot F.G. Adventures of a pore-forming toxin at the target cell surface. Trends Microbiol. 8 (2000) 168-172
    • (2000) Trends Microbiol. , vol.8 , pp. 168-172
    • Abrami, L.1    Fivaz, M.2    van der Goot, F.G.3
  • 44
    • 1842689787 scopus 로고    scopus 로고
    • The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin
    • Melton J.A., Parker M.W., Rossjohn J., Buckley J.T., and Tweten R.K. The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin. J. Biol. Chem. 279 (2004) 14315-14322
    • (2004) J. Biol. Chem. , vol.279 , pp. 14315-14322
    • Melton, J.A.1    Parker, M.W.2    Rossjohn, J.3    Buckley, J.T.4    Tweten, R.K.5
  • 45
    • 32544443056 scopus 로고    scopus 로고
    • A rivet model for channel formation by aerolysin-like pore-forming toxins
    • Iacovache I., Paumard P., Scheib H., Lesieur C., Sakai N., Matile S., et al. A rivet model for channel formation by aerolysin-like pore-forming toxins. EMBO J. 25 (2006) 457-466
    • (2006) EMBO J. , vol.25 , pp. 457-466
    • Iacovache, I.1    Paumard, P.2    Scheib, H.3    Lesieur, C.4    Sakai, N.5    Matile, S.6
  • 46
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson W.R., and Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA 85 (1988) 2444-2448
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 47
    • 0035957956 scopus 로고    scopus 로고
    • Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane
    • Miyata S., Matsushita O., Minami J., Katayama S., Shimamoto S., and Okabe A. Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J. Biol. Chem. 276 (2001) 13778-13783
    • (2001) J. Biol. Chem. , vol.276 , pp. 13778-13783
    • Miyata, S.1    Matsushita, O.2    Minami, J.3    Katayama, S.4    Shimamoto, S.5    Okabe, A.6
  • 49
    • 21644480302 scopus 로고    scopus 로고
    • Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells
    • Akiba T., Abe Y., Kitada S., Kusaka Y., Ito A., Ichimatsu T., et al. Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells. Acta Crystallogr. Sect. D 60 (2004) 2355-2357
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2355-2357
    • Akiba, T.1    Abe, Y.2    Kitada, S.3    Kusaka, Y.4    Ito, A.5    Ichimatsu, T.6
  • 50
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 51
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French G.S., and Wilson K.S. On the treatment of negative intensity observations. Acta Crystallogr. Sect. A 34 (1978) 517-525
    • (1978) Acta Crystallogr. Sect. A , vol.34 , pp. 517-525
    • French, G.S.1    Wilson, K.S.2
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 53
    • 0002584126 scopus 로고
    • Data reduction
    • Sawyer L., Isaacs N.W., and Bailey S. (Eds), SERC Daresbury Laboratory, Warrington, UK
    • Evans P.R. Data reduction. In: Sawyer L., Isaacs N.W., and Bailey S. (Eds). Proceedings of the CCP4 Study Weekend. Data Collection and Processing (1993), SERC Daresbury Laboratory, Warrington, UK 114-122
    • (1993) Proceedings of the CCP4 Study Weekend. Data Collection and Processing , pp. 114-122
    • Evans, P.R.1
  • 54
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • La Fortelle E.d., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276 (1997) 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • La Fortelle, E.d.1    Bricogne, G.2
  • 56
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F-1 ATPase
    • Abrahams J.P., and Leslie A.G.W. Methods used in the structure determination of bovine mitochondrial F-1 ATPase. Acta Crystallogr. Sect. D 52 (1996) 30-42
    • (1996) Acta Crystallogr. Sect. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 57
    • 0002583957 scopus 로고
    • DM: an automated procedure for phase improvement by density modification
    • Cowtan K. DM: an automated procedure for phase improvement by density modification. Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31 (1994) 34-38
    • (1994) Jt. CCP4 ESF-EACBM Newsl. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 58
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 59
    • 0002771888 scopus 로고
    • TURBO-FRODO: a tool for building structural models
    • Silicon Graphics (Ed), Silicon Graphics, Mountain View, CA
    • Roussel A., and Cambillau C. TURBO-FRODO: a tool for building structural models. In: Silicon Graphics (Ed). Silicon Graphics Geometry Partners Directory (1991), Silicon Graphics, Mountain View, CA 86
    • (1991) Silicon Graphics Geometry Partners Directory , pp. 86
    • Roussel, A.1    Cambillau, C.2
  • 61
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 63
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. Sect. D 57 (2001) 122-133
    • (2001) Acta Crystallogr. Sect. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 64
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 65
    • 0026244229 scopus 로고
    • Molscript-a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript-a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.