Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi.
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 P4(1)2(1)2 or enantiomorph with cell dimensions a = b = 108.5 and c = 92.8 A (at 100 K). Native crystals diffract to better than 2.6 A on a synchrotron X-ray source. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 3.6 A(3) Da(-1).
Division of Biochemistry and Molecular Biology, Institute of Biological and Life Sciences, University of Glasgow, Scotland.
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Krell
J E
JE
Coyle
M J
MJ
Horsburgh
J R
JR
Coggins
A J
AJ
Lapthorn