| Title : Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei - Hakulinen_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_430 |
| Author(s) : Hakulinen N , Tenkanen M , Rouvinen J |
| Ref : Acta Crystallographica D Biol Crystallogr , 54 :430 , 1998 |
|
Abstract :
Acetyl xylan esterase is involved in the biodegradation of hemicellulose. It cleaves O-acetyl groups from xylan, which is the most abundant hemicellulose in nature. The catalytic core of acetyl xylan esterase from T. reesei has been crystallized and X-ray diffraction data at 2.3 A collected. The crystal belongs to the triclinic space group P1 with unit-cell parameters a = 50.3, b = 62. 1, c = 40.0 A, alpha = 110.1, beta = 113.6 and gamma = 97.9 degrees. The asymmetric unit contains two molecules. |
| PubMedSearch : Hakulinen_1998_Acta.Crystallogr.D.Biol.Crystallogr_54_430 |
| PubMedID: 9761918 |
| Gene_locus related to this paper: hypje-axylest |
| Gene_locus | hypje-axylest |
Hakulinen N, Tenkanen M, Rouvinen J (1998)
Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei
Acta Crystallographica D Biol Crystallogr
54 :430
Hakulinen N, Tenkanen M, Rouvinen J (1998)
Acta Crystallographica D Biol Crystallogr
54 :430