Crystallization and preliminary X-ray diffraction studies of Bacillus stearothermophilus farnesyl diphosphate synthase expressed in Escherichia coli.
Thermostable farnesyl diphosphate synthase (EC 2.5.1.10) from Bacillus stearothermophilus, which was overexpressed in Escherichia coli, has been crystallized by the vapor-diffusion procedure. Tetragonal crystals were obtained using ammonium sulfate as a precipitant. The crystals diffracted X-rays to about 3 A resolution. The diffraction pattern indicated that the space group is I4(1)22 with unit-cell dimensions of a = b = 114 A and c = 247 A. It is thought that the asymmetric unit comprises two or three molecules of farnesyl diphosphate synthase.
Nakane
H
H
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Koyama
T
T
Obata
S
S
Osabe
M
M
Takeshita
A
A
Nishino
T
T
Ogura
K
K
Miki
K
K
D019883:Alkyl and Aryl Transferases; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli; D001411:Geobacillus stearothermophilus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D051228:Geranyltranstransferase; D014166:Transferases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D014166:Transferases; D019883:Alkyl and Aryl Transferases; D051228:Geranyltranstransferase