P43212

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 279 Experts worldwide ranked by ideXlab platform

William J. Cook - One of the best experts on this subject based on the ideXlab platform.

  • Crystallization and preliminary X-ray investigation of recombinant human interleukin 10.
    Proteins: Structure Function and Genetics, 1995
    Co-Authors: William J. Cook, William T. Windsor, Nicholas J. Murgolo, Stephen Tindall, Tattanahalli L. Nagabhushan, Mark R. Walter
    Abstract:

    Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 A and c = 221.9 A. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X-rays and diffract to at least 2.5 A resolution. © 1995 Wiley-Liss, Inc.

  • CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF RECOMBINANT HUMAN INTERLEUKIN 4
    Journal of Molecular Biology, 1991
    Co-Authors: William J. Cook, Tattanahalli L. Nagabhushan, Steven E. Ealick, Paul Reichert, Gerald S. Hammond, Paul P. Trotta, Charles E. Bugg
    Abstract:

    Crystals of recombinant human interleukin 4 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space-group P41212 or P43212; the unit cell axes are a = 92.2(1) A and c = 46.4(1) A. The crystals are stable to X-rays for at least three days and diffract beyond 2.8 A resolution. The crystals contain approximately 63% solvent, assuming there is one molecule in the asymmetric unit.

Tattanahalli L. Nagabhushan - One of the best experts on this subject based on the ideXlab platform.

  • Crystallization and preliminary X-ray investigation of recombinant human interleukin 10.
    Proteins: Structure Function and Genetics, 1995
    Co-Authors: William J. Cook, William T. Windsor, Nicholas J. Murgolo, Stephen Tindall, Tattanahalli L. Nagabhushan, Mark R. Walter
    Abstract:

    Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 A and c = 221.9 A. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X-rays and diffract to at least 2.5 A resolution. © 1995 Wiley-Liss, Inc.

  • CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF RECOMBINANT HUMAN INTERLEUKIN 4
    Journal of Molecular Biology, 1991
    Co-Authors: William J. Cook, Tattanahalli L. Nagabhushan, Steven E. Ealick, Paul Reichert, Gerald S. Hammond, Paul P. Trotta, Charles E. Bugg
    Abstract:

    Crystals of recombinant human interleukin 4 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space-group P41212 or P43212; the unit cell axes are a = 92.2(1) A and c = 46.4(1) A. The crystals are stable to X-rays for at least three days and diffract beyond 2.8 A resolution. The crystals contain approximately 63% solvent, assuming there is one molecule in the asymmetric unit.

Igor Polikarpov - One of the best experts on this subject based on the ideXlab platform.

  • Crystallization and preliminary X-ray diffraction analysis of a novel trypsin inhibitor from seeds of Copaifera langsdorffii.
    Acta Crystallographica Section D Biological Crystallography, 2001
    Co-Authors: Sandra Krauchenco, José Alberto Fracassi Da Silva, Ronaldo Alves Pinto Nagem, J.r. Brandão Neto, V.p. Forrer, R. Carmona E Ferreira, Maria Lígia Rodrigues Macedo, José C. Novello, Sergio Marangoni, Igor Polikarpov
    Abstract:

    A novel trypsin inhibitor isolated from seeds of Copaifera langsdorffii was purified to homogeneity and crystallized. Crystals suitable for X-­ray analysis were grown using the hanging-drop vapour-diffusion method at 291 K in sodium acetate buffer at pH values near 4.3 using PEG 4000 as precipitant. The crystals presented symmetry compatible with the space group P41212 or P43212, with unit-cell parameters a = b = 58.71, c = 93.75 A, and diffracted to 1.83 A resolution at the synchrotron source.

  • Crystallization and preliminary X-ray study of β-­mannosidase from Trichoderma reesei
    Acta Crystallographica Section D Biological Crystallography, 2000
    Co-Authors: Ricardo Aparicio, E. V. Eneiskaya, Anna A. Kulminskaya, Andrew N. Savel'ev, A. M. Golubev, Kirill N. Neustroev, J. Kobarg, Igor Polikarpov
    Abstract:

    β-Mannosidase from Trichoderma reesei, a 105 kDa glycoprotein, has been crystallized. The crystals belong to the space group P41212 or P43212, with unit-cell dimensions a = b = 165.86, c = 122.46 A, and diffract beyond 2.75 A resolution. X-ray diffraction data were collected from a frozen crystal on a synchrotron X-ray source.

Charles E. Bugg - One of the best experts on this subject based on the ideXlab platform.

  • CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF RECOMBINANT HUMAN INTERLEUKIN 4
    Journal of Molecular Biology, 1991
    Co-Authors: William J. Cook, Tattanahalli L. Nagabhushan, Steven E. Ealick, Paul Reichert, Gerald S. Hammond, Paul P. Trotta, Charles E. Bugg
    Abstract:

    Crystals of recombinant human interleukin 4 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space-group P41212 or P43212; the unit cell axes are a = 92.2(1) A and c = 46.4(1) A. The crystals are stable to X-rays for at least three days and diffract beyond 2.8 A resolution. The crystals contain approximately 63% solvent, assuming there is one molecule in the asymmetric unit.

Mark R. Walter - One of the best experts on this subject based on the ideXlab platform.