Literature summary extracted from
Momma, M.; Fujimoto, Z.; Maita, N.; Haraguchi, K.; Mizuno, H.
Expression, crystallization and preliminary X-ray crystallographic studies of Arthrobacter globiformis inulin fructotransferase (2003), Acta Crystallogr. Sect. D, D59, 2286-2288.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.2.18 |
overexpression in Escherichia coli |
Arthrobacter globiformis |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.2.18 |
crystals are obtained at 20°C by hanging drop vapour-diffusion method using 0.1 M Na HEPES pH 7.5 buffer containing 1.5 M lithium sulfate as a precipitant. Crystals of the recombinant wild-type enzyme diffract to better than 1.5 A at -173°C. The crystals belong to space group R32, with unit-cell parameters a = b = 90.02 A, c = 229.82 A in the hexagonal axes. Selenomethionine-derivative crystals belong to a different space group, C2, with unit-cell parameters a = 159.32, cb = 91.92, c = 92.58 A, beta = 125.06. The C2 selenomethionine-derived crystal contains three molecules per asymmetric unit |
Arthrobacter globiformis |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.2.2.18 |
43000 |
- |
3 * 43000, SDS-PAGE |
Arthrobacter globiformis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.2.18 |
Arthrobacter globiformis |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.2.18 |
recombinant |
Arthrobacter globiformis |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.2.2.18 |
trimer |
3 * 43000, SDS-PAGE |
Arthrobacter globiformis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.2.18 |
IFTaseIII |
- |
Arthrobacter globiformis |
4.2.2.18 |
inulin fructotransferase (DFAIII-producing) |
- |
Arthrobacter globiformis |