Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli

Maclean, J., Campbell, S. A., Pollock, K., Chackrewarthy, S., Coggins, J. R. and Lapthorn, A. J. (2000) Crystallization and preliminary X-ray analysis of shikimate dehydrogenase fromEscherichia coli. Acta Crystallographica. Section D: Biological Crystallography, 56(4), pp. 512-515. (doi: 10.1107/S0907444900002377)

Abstract

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.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Lapthorn, Dr Adrian and Coggins, Professor John
• Authors: Maclean, J., Campbell, S. A., Pollock, K., Chackrewarthy, S., Coggins, J. R., and Lapthorn, A. J.
• College/School: College of Medical Veterinary and Life Sciences > School of Life Sciences; College of Science and Engineering > School of Chemistry
• Journal Name: Acta Crystallographica. Section D: Biological Crystallography
• Publisher: International Union of Crystallography
• ISSN: 0907-4449
• ISSN (Online): 1399-0047