| Title : Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha\/beta-hydrolase-fold superfamily - Steiner_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_382 |
| Author(s) : Steiner RA , Frerichs-Deeken U , Fetzner S |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :382 , 2007 |
|
Abstract :
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the alpha/beta-hydrolase-fold superfamily of enzymes. N-terminally His6-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 A resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 153.788, c = 120.872 A. |
| PubMedSearch : Steiner_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_382 |
| PubMedID: 17565176 |
| Gene_locus related to this paper: artsp-hod |
| Gene_locus | artsp-hod |
Steiner RA, Frerichs-Deeken U, Fetzner S (2007)
Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha\/beta-hydrolase-fold superfamily
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :382
Steiner RA, Frerichs-Deeken U, Fetzner S (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :382