Crystallization and preliminary X-ray studies of D-serine dehydratase from Escherichia coli.
Single crystals of D-serine dehydratase from Escherichia coli complexed with 3-amino-2-hydroxypropionate have been obtained from ammonium sulfate solution (pH 7.0) by vapor diffusion. The crystals belong to the trigonal space group P3(1) or P3(2) with a = b = 81.3 A and c = 58.4 A. The asymmetric unit cell contains one protein molecule with Mr = 48,289. The crystals diffract to at least 3.0 A resolution and are suitable for X-ray structure analysis.
Obmolova
G
G
Institute of Crystallography, Academy of Sciences of the U.S.S.R., Moscow.
Tepliakov
A
A
Harutyunyan
E
E
Wahler
G
G
Schnackerz
K D
KD
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D012695:L-Serine Dehydratase; D014961:X-Ray Diffraction
D012695:L-Serine Dehydratase