Research Output
Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli
  Shikimate dehydrogenase from Escherichia coli has been crystallized by the vapour-diffusion method using ammonium sulfate as a precipitant. Mass spectrometry confirmed the purity of the enzyme and dynamic light scattering was used to find the appropriate additives to yield a monodisperse enzyme solution. The crystals are monoclinic, space group C2, with unit-cell parameters a = 110.0, b = 139.8, c = 102.6 Å, [beta] = 122.2° (at 100 K). Native crystals diffract to 2.3 Å in-house on a rotating-anode X-ray source. The asymmetric unit is likely to contain four molecules, related by 222 symmetry, corresponding to a packing density of 2.86 Å3 Da-1.

  • Type:

    Article

  • Date:

    01 April 2000

  • Publication Status:

    Published

  • Publisher

    International Union of Crystallography/ Wiley

  • DOI:

    10.1107/s0907444900002377

  • Cross Ref:

    S0907444900002377

  • ISSN:

    0907-4449

  • Library of Congress:

    QH301 Biology

Citation

Maclean, J., Campbell, S. A., Pollock, K., Chackrewarthy, S., Coggins, J. R., & Lapthorn, A. J. (2000). Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli. Acta crystallographica. Section D, Biological crystallography, 56(4), 512-515. https://doi.org/10.1107/s0907444900002377

Authors

Keywords

antimicrobials; oxidoreductases; shikimate dehydrogenase; shikimate pathway;

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