title: Expression, crystallization and preliminary X-ray analysis of rice L-galactose dehydrogenase.
abstract: In plants, L-galactose dehydrogenase (L-GalDH) is a key enzyme in the biosynthesis of ascorbic acid (AsA), which is well known as a unique antioxidant compound and a cofactor for many enzymes. L-GalDH catalyses the oxidation of L-galactose to L-galactono-1,4-lactone. Rice L-GalDH was overexpressed in Escherichia coli, purified and crystallized. Diffraction-quality rod-shaped crystals were grown using a sitting-drop vapour-diffusion method. The L-GalDH crystals exhibited the symmetry of space group P21 and diffracted to a resolution of 1.2 Å. The crystals had unit-cell parameters a = 46.8, b = 54.9, c = 56.9 Å, β = 102.3°. On the basis of the Matthews coefficient (VM = 2.1 Å(3) Da(-1), solvent content of 42.3%), it was estimated that one peptide was present in the asymmetric unit.
authors.affiliation: Biomolecular Research Unit, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba 305-8602, Japan. momma@affrc.go.jp
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Momma
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D005691:Galactose Dehydrogenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012275:Oryza / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D005691:Galactose Dehydrogenases; C047959:galactose dehydrogenase
keywords: Oryza sativa L.; ascorbic acid biosynthesis; l-galactose dehydrogenase