Literature summary extracted from
Are, V.; Ghosh, B.; Kumar, A.; Yadav, P.; Bhatnagar, D.; Jamdar, S.; Makde, R.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of acylpeptide hydrolase from Deinococcus radiodurans (2014), Acta Crystallogr. Sect. F, 70, 1292-1295.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
3.4.19.1 |
expressed in Escherichia coli |
Deinococcus radiodurans |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.19.1 |
crystallized using microbatch-under-oil employing the random microseed matrix screening method. The protein crystallizes in space group P2(1)1, with unit-cell parameters a: 77.6, b: 189.6, c: 120.4 A, beta: 108.4 |
Deinococcus radiodurans |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.4.19.1 |
73000 |
- |
4 * 73000 |
Deinococcus radiodurans |
3.4.19.1 |
265000 |
- |
gel filtration |
Deinococcus radiodurans |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.19.1 |
Deinococcus radiodurans |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.19.1 |
using gel filtration |
Deinococcus radiodurans |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.4.19.1 |
tetramer |
4 * 73000 |
Deinococcus radiodurans |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.19.1 |
APHdr |
- |
Deinococcus radiodurans |