Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase fromErwinia chrysanthemi

Krell, T., Coyle, J. E., Horsburgh, M. J., Coggins, J. R. and Lapthorn, A. J. (1997) Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase fromErwinia chrysanthemi. Acta Crystallographica. Section D: Biological Crystallography, 53(5), pp. 612-614. (doi: 10.1107/S0907444997004319)

Abstract

Shikimate kinase from Erwinia chrysanthemi, overexpressed in Escherichia coli has been crystallized by the vapour-diffusion method using sodium chloride as a precipitant. Mass spectrometry was used to confirm the purity of the shikimate kinase and dynamic light scattering was used to assess conditions for the monodispersity of the enzyme. The crystals are tetragonal, space group P41212 or enantiomorph with cell dimensions a = b = 108.5 and c = 92.8 Å (at 100 K). Native crystals diffract to better than 2.6 Å on a synchrotron X-ray source. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 3.6 Å3 Da-1.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Lapthorn, Dr Adrian and Coggins, Professor John
• Authors: Krell, T., Coyle, J. E., Horsburgh, M. J., 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