Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia 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 A, beta = 122.2 degrees (at 100 K). Native crystals diffract to 2.3 A 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(3) Da(-1).
Maclean
J
J
Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland.
Campbell
S A
SA
Pollock
K
K
Chackrewarthy
S
S
Coggins
J R
JR
Lapthorn
A J
AJ
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D013058:Mass Spectrometry; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase