| Title : Crystallization and preliminary crystallographic analysis of a haloalkane dehalogenase, DbjA, from Bradyrhizobium japonicum USDA110 - Sato_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_294 |
| Author(s) : Sato Y , Natsume R , Tsuda M , Damborsky J , Nagata Y , Senda T |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 63 :294 , 2007 |
|
Abstract :
Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. The haloalkane dehalogenase DbjA constitutes a novel substrate-specificity class with high catalytic activity for beta-methylated haloalkanes. In order to reveal the mechanism of its substrate specificity, DbjA has been crystallized using the hanging-drop vapour-diffusion method. The best crystals were obtained using the microseeding technique with a reservoir solution consisting of 17-19.5%(w/v) PEG 4000, 0.2 M calcium acetate and 0.1 M Tris-HCl pH 7.7-8.0. The space group of the DbjA crystal is P2(1)2(1)2, with unit-cell parameters a = 212.9, b = 117.8, c = 55.8 A. The crystal diffracts to 1.75 A resolution. |
| PubMedSearch : Sato_2007_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_63_294 |
| PubMedID: 17401198 |
Sato Y, Natsume R, Tsuda M, Damborsky J, Nagata Y, Senda T (2007)
Crystallization and preliminary crystallographic analysis of a haloalkane dehalogenase, DbjA, from Bradyrhizobium japonicum USDA110
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :294
Sato Y, Natsume R, Tsuda M, Damborsky J, Nagata Y, Senda T (2007)
Acta Crystallographica Sect F Struct Biol Cryst Commun
63 :294