Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110

Authors

Sato, Y., Natsume, R., Tsuda, M., Damborsky, J., Nagata, Y., Senda, T.

Source

ACTA CRYSTALLOGRAPHICA SECTION F 63: 294-296 (2007)

Abstract

Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. A haloalkane dehalogenase, DbjA, constitutes a novel substrate specificity class with high catalytic activity for beta-methylated haloalkanes. In order to reveal the mechanism of the substrate specificity, DbjA has been crystallized by the hanging drop vapor diffusion method. The best crystals were obtained by the microseeding technique with a reservoir solution 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 P212?2 with unit cell parameters a=212.85 A, b=117.84 A, c=55.80 A. The crystal diffracts to 1.75 A resolution.

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Citation

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 Section F 63: 294-296.

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