| Title : Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus - Liu_2000_Acta.Crystallogr.D.Biol.Crystallogr_56_900 |
| Author(s) : Liu JW , Verger D , Carr PD , Yang H , Ollis DL |
| Ref : Acta Crystallographica D Biol Crystallogr , 56 :900 , 2000 |
|
Abstract :
An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the alpha/beta hydrolase fold. The crystals diffract to 2.8 A and belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 A. |
| PubMedSearch : Liu_2000_Acta.Crystallogr.D.Biol.Crystallogr_56_900 |
| PubMedID: 10930838 |
Liu JW, Verger D, Carr PD, Yang H, Ollis DL (2000)
Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus
Acta Crystallographica D Biol Crystallogr
56 :900
Liu JW, Verger D, Carr PD, Yang H, Ollis DL (2000)
Acta Crystallographica D Biol Crystallogr
56 :900