Literature summary extracted from
Katsumi, R.; Koga, Y.; You, D.J.; Matsumura, H.; Takano, K.; Kanaya, S.
Crystallization and preliminary x-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis (2007), Acta Crystallogr. Sect. F, F63, 126-129.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.1.30 |
overproduced in Escherichia coli BL21 (DE3) |
Thermococcus kodakarensis |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.1.30 |
using sitting-drop vapour-diffusion method at 293 K. Native Tk-glycerol kinase crystals appear after a few days using Wizard I solution No. 25 (0.1 M Tris pH 8.5, 0.2 M MgCl2, 30% PEG 400). Diffraction spots sufficient for structural determination at high resolution are not obtained when a crystal of Tk-glycerol kinase is mounted on a CryoLoop without cryoprotectant, diffraction patterns of the crystal are improved by using Paratone-N as cryoprotectant. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystals belong 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 VM value is 2.7 A3Da-1 and the solvent content is 54.1%. |
Thermococcus kodakarensis |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.7.1.30 |
56000 |
- |
SDS-PAGE |
Thermococcus kodakarensis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.1.30 |
Thermococcus kodakarensis |
- |
hyperthermophilic archaeon |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.1.30 |
HiTrapQ HP column, Bio-Scale CHT20-I column, all purification procedures are carried out at 277 K. |
Thermococcus kodakarensis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.1.30 |
GK |
glycerol kinase |
Thermococcus kodakarensis |