Crystals of DhaA Mutants from Rhodococcus rhodochrous NCIMB 13064 Diffracted to Ultrahigh Resolution: Crystallization and Preliminary Diffraction Analysis.

Warning

This publication doesn't include Faculty of Education. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

STSIASPANAVA A. KOUDELÁKOVÁ Táňa LAPKOUSKI M. PAVLOVÁ Martina DAMBORSKÝ Jiří KUTÁ-SMATANOVÁ Ivana

Year of publication 2008
Type Article in Periodical
Magazine / Source Acta Crystallographica Section D: Biological Crystallography
MU Faculty or unit

Faculty of Science

Citation
Web http://loschmidt.chemi.muni.cz/peg/abstracts/acsf08.html
Field Biochemistry
Keywords haloalkane dehalogenases; enzyme DhaA; crystals;
Description The enzyme DhaA from Rhodococcus rhodochrous NCIMB 13064 belongs to the haloalkane dehalogenases, which catalyze the hydrolysis of haloalkanes to the corresponding alcohols. The haloalkane dehalogenase DhaA and its variants can be used to detoxify the industrial pollutant 1,2,3-trichloropropane (TCP). Three mutants named DhaA04, DhaA14 and DhaA15 were constructed in order to study the importance of tunnels connecting the buried active site with the surrounding solvent to the enzymatic activity. All protein mutants were crystallized using the sitting-drop vapour-diffusion method. The crystals of DhaA04 belonged to the orthorhombic space group P212121, while the crystals of the other two mutants DhaA14 and DhaA15 belonged to the triclinic space group P1. Native data sets were collected for the DhaA04, DhaA14 and DhaA15 mutants at beamline X11 of EMBL, DESY, Hamburg to the high resolutions of 1.30, 0.95 and 1.15 A, respectively.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.