Open AccessExpression, crystallization and preliminary X‐ray analysis of rice L‐galactose dehydrogenase
Author(s) -
Momma Mitsuru,
Fujimoto Zui
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113016692
Subject(s) - crystallization , galactose , enzyme , dehydrogenase , escherichia coli , chemistry , cofactor , ascorbic acid , crystallography , solvent , resolution (logic) , stereochemistry , biochemistry , organic chemistry , food science , gene , artificial intelligence , computer science
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 P 2 1 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 ( V M = 2.1 Å 3 Da −1 , solvent content of 42.3%), it was estimated that one peptide was present in the asymmetric unit.