Open AccessCrystallization and preliminary X‐ray diffraction analysis of the putative aldose 1‐epimerase YeaD from Escherichia coli
Author(s) -
You Weijie,
Qiu Xiaoting,
Zhang Yujie,
Ma Jinming,
Gao Yongxiang,
Zhang Xiao,
Niu Liwen,
Teng Maikun
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110024140
Subject(s) - escherichia coli , crystallization , x ray crystallography , x ray , crystallography , chemistry , diffraction , materials science , biochemistry , gene , physics , optics , organic chemistry
Escherichia coli YeaD (ecYeaD) is suggested to be a member of the galactose mutarotase‐like superfamily. Galactose mutarotase is an enzyme that converts α‐galactose to β‐galactose. The known structures of these galactose mutarotase‐like proteins are similar to those of galactose mutarotases, with the catalytic residues being conserved, but there are some differences between them in the substrate‐binding pocket. In order to reveal the specificity of ecYeaD, a three‐dimensional structure is essential. Full‐length ecYeaD with an additional 6×His tag at the C‐terminus was crystallized by the hanging‐drop vapour‐diffusion method using polyethylene glycol 4000 as a precipitant at 283 K. An X‐ray diffraction data set was collected to a resolution of 1.9 Å from a single flash‐cooled crystal that belonged to space group P 2 1 2 1 2 1 .