Development of a Crystallization Protocol for the DbeA1 Variant of Novel Haloalkane Dehalogenase from Bradyrhizobium elkani USDA94-Reference-Cited by-同舟云学术

Development of a Crystallization Protocol for the DbeA1 Variant of Novel Haloalkane Dehalogenase from Bradyrhizobium elkani USDA94

Published:2010-12-31 Issue:2 Volume:11 Page:516-519
ISSN:1528-7483
Container-title:Crystal Growth & Design
language:en
Short-container-title:Crystal Growth & Design

Author:

Prudnikova T.¹,Chaloupkova R.²,Sato Y.³,Nagata Y.³,Degtjarik O.¹,Kuty M.¹⁴,Rezacova P.⁵,Damborsky J.²,Kuta Smatanova I.¹⁴

Affiliation:

1. Institute of Physical Biology, University of South Bohemia in Ceske Budejovice, Zamek 136, 373 33 Nove Hrady, Czech Republic

2. Loschmidt Laboratories, Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic

3. Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Sendai 980-8577, Japan

4. Institute of Systems Biology and Ecology, Academy of Science of Czech Republic, Zamek 136, 373 33 Nove Hrady, Czech Republic

5. Institute of Molecular Genetics, Academy of Sciences of Czech Republic, Videnska 1083, 142 20 Prague 4, Czech Republic

Publisher

American Chemical Society (ACS)

Subject

Condensed Matter Physics,General Materials Science,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cg1013363

Reference17 articles.

1. Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities

2. The Plasmid-Located Haloalkane Dehalogenase Gene from Rhodococcus Rhodochrous NCIMB 13064

3. Refined X-ray Structures of Haloalkane Dehalogenase at pH 6·2 and pH 8·2 and Implications for the Reaction Mechanism

4. Haloalkane Dehalogenases: Structure of a Rhodococcus Enzyme,

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