Filtros : "Polikarpov, Igor" "Dinamarca" Removidos: "ROCHA, PAULO ARCHIAS MENDES DA" "PROGRAMA DE COMPUTADOR" Limpar

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  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, PROTEÍNAS (ESTRUTURA), MOLÉCULA

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      NAGEM, Ronaldo Alves Pinto et al. Getting the most out of X-ray home sources. Acta Crystallographica D, v. 61, p. 1022-1030, 2005Tradução . . Disponível em: https://doi.org/10.1107/s0907444905012989. Acesso em: 24 jun. 2024.
    • APA

      Nagem, R. A. P., Ambrosio, A. L. B., Rojas, A. L., Navarro, M. V. de A. S., Golubev, A. M., Garratt, R. C., & Polikarpov, I. (2005). Getting the most out of X-ray home sources. Acta Crystallographica D, 61, 1022-1030. doi:10.1107/s0907444905012989
    • NLM

      Nagem RAP, Ambrosio ALB, Rojas AL, Navarro MV de AS, Golubev AM, Garratt RC, Polikarpov I. Getting the most out of X-ray home sources [Internet]. Acta Crystallographica D. 2005 ; 61 1022-1030.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444905012989
    • Vancouver

      Nagem RAP, Ambrosio ALB, Rojas AL, Navarro MV de AS, Golubev AM, Garratt RC, Polikarpov I. Getting the most out of X-ray home sources [Internet]. Acta Crystallographica D. 2005 ; 61 1022-1030.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444905012989
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALIZAÇÃO, HORMÔNIOS TIREOIDIANOS

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      NUNES, F. M. et al. Crystallization and preliminary X-ray diffraction studies of isoform 'alfa'1 of the human thyroid hormone receptor ligand-binding domain. Acta Crystallographica D, v. D60, p. 1867-1870, 2004Tradução . . Disponível em: https://doi.org/10.1107/S0907444904017858. Acesso em: 24 jun. 2024.
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      Nunes, F. M., Aparicio, R., Santos, M. A. M., Portugal, R. V., Dias, S. M. G., Neves, F. A. R., et al. (2004). Crystallization and preliminary X-ray diffraction studies of isoform 'alfa'1 of the human thyroid hormone receptor ligand-binding domain. Acta Crystallographica D, D60, 1867-1870. doi:10.1107/S0907444904017858
    • NLM

      Nunes FM, Aparicio R, Santos MAM, Portugal RV, Dias SMG, Neves FAR, Simeoni LA, Baxter JD, Webb P, Polikarpov I. Crystallization and preliminary X-ray diffraction studies of isoform 'alfa'1 of the human thyroid hormone receptor ligand-binding domain [Internet]. Acta Crystallographica D. 2004 ; D60 1867-1870.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/S0907444904017858
    • Vancouver

      Nunes FM, Aparicio R, Santos MAM, Portugal RV, Dias SMG, Neves FAR, Simeoni LA, Baxter JD, Webb P, Polikarpov I. Crystallization and preliminary X-ray diffraction studies of isoform 'alfa'1 of the human thyroid hormone receptor ligand-binding domain [Internet]. Acta Crystallographica D. 2004 ; D60 1867-1870.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/S0907444904017858
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, CRISTALIZAÇÃO, HIV, SÍNDROME DE IMUNODEFICIÊNCIA ADQUIRIDA, MUTAÇÃO, VÍRUS, BIOFÍSICA

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      SANCHES, Mario et al. Crystallization of a non-B and a B mutant HIV protease. Acta Crystallographica D, v. D60, p. Se 2004, 2004Tradução . . Disponível em: https://doi.org/10.1107/s0907444904015276. Acesso em: 24 jun. 2024.
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      Sanches, M., Martins, N. H., Calazans, A., Brindeiro, R. de M., Tanuri, A., Antunes, O. A. C., & Polikarpov, I. (2004). Crystallization of a non-B and a B mutant HIV protease. Acta Crystallographica D, D60, Se 2004. doi:10.1107/s0907444904015276
    • NLM

      Sanches M, Martins NH, Calazans A, Brindeiro R de M, Tanuri A, Antunes OAC, Polikarpov I. Crystallization of a non-B and a B mutant HIV protease [Internet]. Acta Crystallographica D. 2004 ; D60 Se 2004.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444904015276
    • Vancouver

      Sanches M, Martins NH, Calazans A, Brindeiro R de M, Tanuri A, Antunes OAC, Polikarpov I. Crystallization of a non-B and a B mutant HIV protease [Internet]. Acta Crystallographica D. 2004 ; D60 Se 2004.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444904015276
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, SEQUÊNCIA DE AMINOÁCIDOS, ENZIMAS, PROTEÍNAS, VENENOS DE ORIGEM ANIMAL

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      RIGDEN, Daniel J. et al. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding. Acta Crystallographica D, v. 59, p. 255-262, 2003Tradução . . Disponível em: https://doi.org/10.1107/s0907444902021467. Acesso em: 24 jun. 2024.
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      Rigden, D. J., Lee, W. -H., Marangoni, S., Toyama, M. H., & Polikarpov, I. (2003). The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding. Acta Crystallographica D, 59, 255-262. doi:10.1107/s0907444902021467
    • NLM

      Rigden DJ, Lee W-H, Marangoni S, Toyama MH, Polikarpov I. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding [Internet]. Acta Crystallographica D. 2003 ; 59 255-262.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902021467
    • Vancouver

      Rigden DJ, Lee W-H, Marangoni S, Toyama MH, Polikarpov I. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding [Internet]. Acta Crystallographica D. 2003 ; 59 255-262.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902021467
  • Source: Acta Crystallographica D. Unidades: FCF, IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS

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    • ABNT

      SANCHES, Mario et al. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups. Acta Crystallographica D, v. 59, p. 416-422, 2003Tradução . . Disponível em: https://doi.org/10.1107/s0907444902021200. Acesso em: 24 jun. 2024.
    • APA

      Sanches, M., Barbosa, J. A. R. G., Oliveira, R. T., Abrahão Neto, J., & Polikarpov, I. (2003). Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups. Acta Crystallographica D, 59, 416-422. doi:10.1107/s0907444902021200
    • NLM

      Sanches M, Barbosa JARG, Oliveira RT, Abrahão Neto J, Polikarpov I. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups [Internet]. Acta Crystallographica D. 2003 ; 59 416-422.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902021200
    • Vancouver

      Sanches M, Barbosa JARG, Oliveira RT, Abrahão Neto J, Polikarpov I. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups [Internet]. Acta Crystallographica D. 2003 ; 59 416-422.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902021200
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, TOXINAS

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      PINHEIRO, Carlos Basílio et al. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels. Acta Crystallographica D, v. 59, p. 405-415, 2003Tradução . . Disponível em: https://doi.org/10.1107/s090744490202111x. Acesso em: 24 jun. 2024.
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      Pinheiro, C. B., Marangoni, S., Toyama, M. H., & Polikarpov, I. (2003). Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels. Acta Crystallographica D, 59, 405-415. doi:10.1107/s090744490202111x
    • NLM

      Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels [Internet]. Acta Crystallographica D. 2003 ; 59 405-415.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s090744490202111x
    • Vancouver

      Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels [Internet]. Acta Crystallographica D. 2003 ; 59 405-415.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s090744490202111x
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: BIOQUÍMICA ORGÂNICA, FÍSICA DA MATÉRIA CONDENSADA

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      NAGEM, R. A. P. et al. Crystallization and synchrotron X-ray diffraction studies of human interleukin-22. Acta Crystallographica D, v. 58, p. 529-530, 2002Tradução . . Disponível em: https://doi.org/10.1107/s0907444902001063. Acesso em: 24 jun. 2024.
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      Nagem, R. A. P., Lucchesi, K. W., Colau, D., Dumoutier, L., Renauld, J. C., & Polikarpov, I. (2002). Crystallization and synchrotron X-ray diffraction studies of human interleukin-22. Acta Crystallographica D, 58, 529-530. doi:10.1107/s0907444902001063
    • NLM

      Nagem RAP, Lucchesi KW, Colau D, Dumoutier L, Renauld JC, Polikarpov I. Crystallization and synchrotron X-ray diffraction studies of human interleukin-22 [Internet]. Acta Crystallographica D. 2002 ;58 529-530.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902001063
    • Vancouver

      Nagem RAP, Lucchesi KW, Colau D, Dumoutier L, Renauld JC, Polikarpov I. Crystallization and synchrotron X-ray diffraction studies of human interleukin-22 [Internet]. Acta Crystallographica D. 2002 ;58 529-530.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902001063
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, PROTEÍNAS, VENENOS DE ORIGEM ANIMAL

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      WATANABE, L. et al. Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus. Acta Crystallographica D, v. 58, p. 1879-1881, 2002Tradução . . Disponível em: https://doi.org/10.1107/s0907444902011022. Acesso em: 24 jun. 2024.
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      Watanabe, L., Nirthanan, S., Rajaseger, G., Polikarpov, I., Kini, R. M., & Arni, R. K. (2002). Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus. Acta Crystallographica D, 58, 1879-1881. doi:10.1107/s0907444902011022
    • NLM

      Watanabe L, Nirthanan S, Rajaseger G, Polikarpov I, Kini RM, Arni RK. Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus [Internet]. Acta Crystallographica D. 2002 ; 58 1879-1881.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902011022
    • Vancouver

      Watanabe L, Nirthanan S, Rajaseger G, Polikarpov I, Kini RM, Arni RK. Crystallization and preliminary X-ray analysis of bucain, a novel toxin from the Malayan krait Bungarus candidus [Internet]. Acta Crystallographica D. 2002 ; 58 1879-1881.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902011022
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS

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      LEE, Wen-Hwa et al. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallographica D, v. 58, p. 798-804, 2002Tradução . . Disponível em: https://doi.org/10.1107/s0907444902003918. Acesso em: 24 jun. 2024.
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      Lee, W. -H., Perles, L. A., Nagem, R. A. P., Shrive, A. K., Hawkins, A., Sawyer, L., & Polikarpov, I. (2002). Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallographica D, 58, 798-804. doi:10.1107/s0907444902003918
    • NLM

      Lee W-H, Perles LA, Nagem RAP, Shrive AK, Hawkins A, Sawyer L, Polikarpov I. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity [Internet]. Acta Crystallographica D. 2002 ; 58 798-804.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902003918
    • Vancouver

      Lee W-H, Perles LA, Nagem RAP, Shrive AK, Hawkins A, Sawyer L, Polikarpov I. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity [Internet]. Acta Crystallographica D. 2002 ; 58 798-804.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0907444902003918
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: BIOQUÍMICA ORGÂNICA, FÍSICA DA MATÉRIA CONDENSADA

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      KUSER, Fabio R. et al. The X-ray structure of a recombinant major urinary protein at 1.75 'angstron' resolution. A comparative study of X-ray and NMR-derived structures. Acta Crystallographica D, v. 57, p. 1863-1869, 2001Tradução . . Disponível em: https://doi.org/10.1107/S090744490101825X. Acesso em: 24 jun. 2024.
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      Kuser, F. R., Franzoni, L., Ferrari, E., Spisni, A., & Polikarpov, I. (2001). The X-ray structure of a recombinant major urinary protein at 1.75 'angstron' resolution. A comparative study of X-ray and NMR-derived structures. Acta Crystallographica D, 57, 1863-1869. doi:10.1107/S090744490101825X
    • NLM

      Kuser FR, Franzoni L, Ferrari E, Spisni A, Polikarpov I. The X-ray structure of a recombinant major urinary protein at 1.75 'angstron' resolution. A comparative study of X-ray and NMR-derived structures [Internet]. Acta Crystallographica D. 2001 ; 57 1863-1869.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/S090744490101825X
    • Vancouver

      Kuser FR, Franzoni L, Ferrari E, Spisni A, Polikarpov I. The X-ray structure of a recombinant major urinary protein at 1.75 'angstron' resolution. A comparative study of X-ray and NMR-derived structures [Internet]. Acta Crystallographica D. 2001 ; 57 1863-1869.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/S090744490101825X
  • Source: Acta Crystallographica Section D: Biological Crystallography. Unidade: FCF

    Subjects: ESCHERICHIA, ENZIMAS, BIOTECNOLOGIA

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      POLIKARPOV, Igor e OLIVEIRA, R. T. e ABRAHÃO NETO, José. Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography, v. 55, p. 1616-1617, 1999Tradução . . Acesso em: 24 jun. 2024.
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      Polikarpov, I., Oliveira, R. T., & Abrahão Neto, J. (1999). Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography, 55, 1616-1617.
    • NLM

      Polikarpov I, Oliveira RT, Abrahão Neto J. Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography. 1999 ; 55 1616-1617.[citado 2024 jun. 24 ]
    • Vancouver

      Polikarpov I, Oliveira RT, Abrahão Neto J. Preparation and preliminary X-ray diffraction studies of a new crystal form of L-asparaginase from Escherichia coli. Acta Crystallographica Section D: Biological Crystallography. 1999 ; 55 1616-1617.[citado 2024 jun. 24 ]
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: INSTRUMENTAÇÃO (FÍSICA), PROTEÍNAS

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      TEPLYAKOV, A e OLIVA, Glaucius e POLIKARPOV, Igor. On the choice of an optimal wavelength in macromolecular crystallography. Acta Crystallographica D, v. 54, p. 610-614, 1998Tradução . . Acesso em: 24 jun. 2024.
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      Teplyakov, A., Oliva, G., & Polikarpov, I. (1998). On the choice of an optimal wavelength in macromolecular crystallography. Acta Crystallographica D, 54, 610-614.
    • NLM

      Teplyakov A, Oliva G, Polikarpov I. On the choice of an optimal wavelength in macromolecular crystallography. Acta Crystallographica D. 1998 ; 54 610-614.[citado 2024 jun. 24 ]
    • Vancouver

      Teplyakov A, Oliva G, Polikarpov I. On the choice of an optimal wavelength in macromolecular crystallography. Acta Crystallographica D. 1998 ; 54 610-614.[citado 2024 jun. 24 ]
  • Source: Journal of Synchrotron Radiation. Unidade: IF

    Assunto: CRISTALOGRAFIA

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      POLIKARPOV, Igor et al. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory. Journal of Synchrotron Radiation, v. 5, p. 72-76, 1998Tradução . . Disponível em: https://doi.org/10.1107/s0909049597014684. Acesso em: 24 jun. 2024.
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      Polikarpov, I., Perles, L. A., Oliveira, R. T., Oliva, G., Castellano, E. E., Garratt, R. C., & Craievich, A. F. (1998). Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory. Journal of Synchrotron Radiation, 5, 72-76. doi:10.1107/s0909049597014684
    • NLM

      Polikarpov I, Perles LA, Oliveira RT, Oliva G, Castellano EE, Garratt RC, Craievich AF. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory [Internet]. Journal of Synchrotron Radiation. 1998 ; 5 72-76.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0909049597014684
    • Vancouver

      Polikarpov I, Perles LA, Oliveira RT, Oliva G, Castellano EE, Garratt RC, Craievich AF. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory [Internet]. Journal of Synchrotron Radiation. 1998 ; 5 72-76.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0909049597014684
  • Source: Journal of Synchrotron Radiation. Unidade: IFSC

    Subjects: INSTRUMENTAÇÃO (FÍSICA), CRISTALOGRAFIA, PROTEÍNAS

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      POLIKARPOV, Igor et al. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory. Journal of Synchrotron Radiation, v. 5, p. 72-76, 1998Tradução . . Disponível em: https://doi.org/10.1107/s0909049597014684. Acesso em: 24 jun. 2024.
    • APA

      Polikarpov, I., Perles, L. A., Oliveira, R. T., Oliva, G., Castellano, E. E., Garratt, R. C., & Craievich, A. (1998). Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory. Journal of Synchrotron Radiation, 5, 72-76. doi:10.1107/s0909049597014684
    • NLM

      Polikarpov I, Perles LA, Oliveira RT, Oliva G, Castellano EE, Garratt RC, Craievich A. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory [Internet]. Journal of Synchrotron Radiation. 1998 ; 5 72-76.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0909049597014684
    • Vancouver

      Polikarpov I, Perles LA, Oliveira RT, Oliva G, Castellano EE, Garratt RC, Craievich A. Set-up and experimental parameters of the protein crystallography beamline at the Brazilian National Synchrotron Laboratory [Internet]. Journal of Synchrotron Radiation. 1998 ; 5 72-76.[citado 2024 jun. 24 ] Available from: https://doi.org/10.1107/s0909049597014684
  • Source: Acta Chrystallographica D. Unidade: IFSC

    Subjects: INSTRUMENTAÇÃO (FÍSICA), PROTEÍNAS

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      POLIKARPOV, Igor e TEPLYAKOV, A e OLIVA, Glaucius. The ultimate wavelength for protein crystallography?. Acta Chrystallographica D, v. 53, p. 734-737, 1997Tradução . . Acesso em: 24 jun. 2024.
    • APA

      Polikarpov, I., Teplyakov, A., & Oliva, G. (1997). The ultimate wavelength for protein crystallography? Acta Chrystallographica D, 53, 734-737.
    • NLM

      Polikarpov I, Teplyakov A, Oliva G. The ultimate wavelength for protein crystallography? Acta Chrystallographica D. 1997 ; 53 734-737.[citado 2024 jun. 24 ]
    • Vancouver

      Polikarpov I, Teplyakov A, Oliva G. The ultimate wavelength for protein crystallography? Acta Chrystallographica D. 1997 ; 53 734-737.[citado 2024 jun. 24 ]

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