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 con®rmed the purity of the enzyme
and dynamic light scattering was used to ®nd 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 A Ê , � = 122.2� (at 100 K). Native crystals diffract to
2.3 A Ê 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 A Ê 3 Da
ÿ1.

  • Type:

    Article

  • Date:

    09 February 2000

  • Publication Status:

    Published

  • Publisher

    International Union of Crystallography/ Wiley

  • DOI:

    10.1107/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, 512-515. doi:10.1107/S0907444900002377. ISSN 0907-4449

Authors

Keywords

antimicrobials; oxidoreductases; shikimate dehydrogenase; shikimate pathway;

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