L. Kraft et al., Crystallization and preliminary X-ray crystallographic studies of recombinant thermoresistant gluconate kinase GntK from Escherichia coli, ACT CRYST D, 57, 2001, pp. 1159-1161
The thermoresistant gluconate kinase GntK from Escherichia coli, an essenti
al enzyme in gluconate metabolism, has been expressed, purified and crystal
lized. For crystallization, the hanging-drop vapour-diffusion method was us
ed with polyethylene glycol (PEG) 6000 and lithium chloride as precipitants
. Three crystal forms belonging to the monoclinic space group C2 or the ort
horhombic space groups P2(1)2(1)2(1) and P2(1)2(1)2 were obtained. The unit
-cell parameters are a = 75.0, b = 79.3, c = 70.2 Angstrom, beta = 105.3 de
grees (C2), a = 52.0, b = 79.3, c = 89.8 Angstrom (P2(1)2(1)2(1)) and a = 7
0.1, b = 74.1, c = 78.9 Angstrom (P2(1)2(1)2). In all three crystal forms,
there are two molecules in the asymmetric unit; the different forms occur i
n the same crystallization drop. The crystals diffract to at least 2.0 Angs
trom using synchrotron radiation.