| Title : Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha\/beta-hydrolase family - Qi_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_378 |
| Author(s) : Qi R , Fetzner S , Oakley AJ |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :378 , 2007 |
| Abstract : 1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 catalyses the oxygenolysis of 1H-3-hydroxy-4-oxoquinoline to form N-formylanthranilic acid and carbon monoxide without the aid of cofactors. Both N-terminally His6-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His6-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6(1)22. Selenomethionine-containing native QDO was prepared and crystallized under identical conditions. The unit-cell parameters were a = b = 90.1, c = 168.6 A, alpha = beta = 90, gamma = 120 degrees. Using synchrotron radiation, these crystals diffract to 2.5 A. The expression, purification and crystallization of QDO are reported here. |
| ESTHER : Qi_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_378 |
| PubMedSearch : Qi_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_378 |
| PubMedID: 17565175 |
Qi R, Fetzner S, Oakley AJ (2007)
Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha\/beta-hydrolase family
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :378
Qi R, Fetzner S, Oakley AJ (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :378