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

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F07%3A00022814" target="_blank" >RIV/00216224:14310/07:00022814 - isvavai.cz</a>
Result on the web
—
DOI - Digital Object Identifier
—

Result language
angličtina
Original language name
Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110.
Original language description
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.
Czech name
Krystalizace a zakladní krystalografická analýza haloalkan dehalogenázy DbjA z bakterie Bradyrhizobium japonicum USDA110.
Czech description
xxx

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
<a href="/en/project/LC06010" target="_blank" >LC06010: Center of Biocatalysis and Biotransformation</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2007
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Similar results(10)