Crystallization and preliminary X-ray diffraction analysis of the putative aldose 1-epimerase YeaD from Escherichia coli.
Escherichia coli YeaD (ecYeaD) is suggested to be a member of the galactose mutarotase-like superfamily. Galactose mutarotase is an enzyme that converts alpha-galactose to beta-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 6xHis 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 A from a single flash-cooled crystal that belonged to space group P2(1)2(1)2(1).
You
Weijie
W
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, People's Republic of China.
Qiu
Xiaoting
X
Zhang
Yujie
Y
Ma
Jinming
J
Gao
Yongxiang
Y
Zhang
Xiao
X
Niu
Liwen
L
Teng
Maikun
M
D002238:Carbohydrate Epimerases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*
D002238:Carbohydrate Epimerases; C019646:aldose 1-epimerase