Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis.
Glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis was crystallized and preliminary crystallographic studies of the crystals were performed. Crystals were grown at 293 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. Assuming the presence of two molecules in the asymmetric unit, the V(M) value was 2.7 A(3) Da(-1) and the solvent content was 54.1%. The protein was also cocrystallized with substrates and diffraction data were collected to 2.7 A resolution.
Katsumi
Ryota
R
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Koga
Yuichi
Y
You
Dong-Ju
DJ
Matsumura
Hiroyoshi
H
Takano
Kazufumi
K
Kanaya
Shigenori
S
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005990:Glycerol / Q000737:chemistry / Q000378:metabolism; D005991:Glycerol Kinase / Q000737:chemistry* / Q000378:metabolism; D006358:Hot Temperature; D019712:Thermococcus / Q000201:enzymology*
D019843:Archaeal Proteins; D000255:Adenosine Triphosphate; D005991:Glycerol Kinase; D005990:Glycerol