title: Crystallization and preliminary X-ray analysis of shikimate dehydrogenase from Escherichia coli.
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 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).
authors.affiliation: Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, Scotland.
authors.forename: J
authors.initials: J
authors.lastname: Maclean
authors.forename: S A
authors.initials: SA
authors.lastname: Campbell
authors.forename: K
authors.initials: K
authors.lastname: Pollock
authors.forename: S
authors.initials: S
authors.lastname: Chackrewarthy
authors.forename: J R
authors.initials: JR
authors.lastname: Coggins
authors.forename: A J
authors.initials: AJ
authors.lastname: Lapthorn
mesh_terms: 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
chemical_list: D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase