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

J 2007

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

SATO, Yukari, Rio NATSUME, M. TSUDA, Jiří DAMBORSKÝ, Yuji NAGATA et. al.

Základní údaje

Originální název

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

Název česky

Krystalizace a zakladní krystalografická analýza haloalkan dehalogenázy DbjA z bakterie Bradyrhizobium japonicum USDA110.

Autoři

SATO, Yukari (392 Japonsko), Rio NATSUME (392 Japonsko), M. TSUDA (392 Japonsko), Jiří DAMBORSKÝ (203 Česká republika, garant), Yuji NAGATA (392 Japonsko) a T. SENDA (392 Japonsko)

Vydání

Acta Crystallographica Section F, 2007, 1744-3091

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 0.645

Kód RIV

RIV/00216224:14310/07:00022814

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000245505800010

Klíčová slova anglicky

Haloalkane dehalogenases; degradation of halogenated aliphatic pollutants; DbjA; crystals

Štítky

crystals, DbjA, Haloalkane dehalogenases

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 19. 3. 2010 12:25, prof. Mgr. Jiří Damborský, Dr.

Anotace

ORIG CZ

V originále

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.

Česky

xxx

Návaznosti

LC06010, projekt VaV

Název: Centrum biokatalýzy a biotransformací

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Centrum biokatalýzy a biotransformací

Citovat

SATO, Yukari, Rio NATSUME, M. TSUDA, Jiří DAMBORSKÝ, Yuji NAGATA a T. SENDA. Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110. Acta Crystallographica Section F. 2007, roč. 63, č. 4, s. 294-296. ISSN 1744-3091.

@article{727109,
   author = {Sato, Yukari and Natsume, Rio and Tsuda, M. and Damborský, Jiří and Nagata, Yuji and Senda, T.},
   article_number = {4},
   keywords = {Haloalkane dehalogenases; degradation of halogenated aliphatic pollutants; DbjA; crystals},
   language = {eng},
   issn = {1744-3091},
   journal = {Acta Crystallographica Section F},
   title = {Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110.},
   url = {http://loschmidt.chemi.muni.cz/peg/abstracts/acsf07.html},
   volume = {63},
   year = {2007}
}

TY  - JOUR
ID  - 727109
AU  - Sato, Yukari - Natsume, Rio - Tsuda, M. - Damborský, Jiří - Nagata, Yuji - Senda, T.
PY  - 2007
TI  - Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110.
JF  - Acta Crystallographica Section F
VL  - 63
IS  - 4
SP  - 294-296
EP  - 294-296
SN  - 17443091
KW  - Haloalkane dehalogenases
KW  - degradation of halogenated aliphatic pollutants
KW  - DbjA
KW  - crystals
UR  - http://loschmidt.chemi.muni.cz/peg/abstracts/acsf07.html
N2  - 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.
ER  -

SATO, Yukari, Rio NATSUME, M. TSUDA, Jiří DAMBORSKÝ, Yuji NAGATA a T. SENDA. Crystallization and Preliminary Crystallographic Analysis of a Haloalkane Dehalogenase DbjA from Bradyrhizobium japonicum USDA110. \textit{Acta Crystallographica Section F}. 2007, roč.~63, č.~4, s.~294-296. ISSN~1744-3091.

Podrobný výpis o publikaci