Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily

R A Steiner; U Frerichs-Deeken; S Fetzner

doi:10.1107/S174430910701353X

Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily

R A Steiner, U Frerichs-Deeken, S Fetzner

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the alpha/beta-hydrolase-fold superfamily of enzymes. N-terminally His(6)-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 angstrom resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 153.788, c=120.872 angstrom

Original language	English
Article number	gj5017
Pages (from-to)	382 - 385
Number of pages	4
Journal	Acta Crystallographica Section F-Structural Biology And Crystallization Communications
Volume	63
Issue number	5
DOIs	https://doi.org/10.1107/S174430910701353X
Publication status	Published - 28 Apr 2007

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Steiner, R. A., Frerichs-Deeken, U., & Fetzner, S. (2007). Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. Acta Crystallographica Section F-Structural Biology And Crystallization Communications, 63(5), 382 - 385. Article gj5017. https://doi.org/10.1107/S174430910701353X

Steiner, R A ; Frerichs-Deeken, U ; Fetzner, S. / Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. In: Acta Crystallographica Section F-Structural Biology And Crystallization Communications. 2007 ; Vol. 63, No. 5. pp. 382 - 385.

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title = "Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily",

abstract = "1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the alpha/beta-hydrolase-fold superfamily of enzymes. N-terminally His(6)-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 angstrom resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 153.788, c=120.872 angstrom",

author = "Steiner, {R A} and U Frerichs-Deeken and S Fetzner",

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Steiner, RA, Frerichs-Deeken, U & Fetzner, S 2007, 'Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily', Acta Crystallographica Section F-Structural Biology And Crystallization Communications, vol. 63, no. 5, gj5017, pp. 382 - 385. https://doi.org/10.1107/S174430910701353X

Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. / Steiner, R A; Frerichs-Deeken, U; Fetzner, S.
In: Acta Crystallographica Section F-Structural Biology And Crystallization Communications, Vol. 63, No. 5, gj5017, 28.04.2007, p. 382 - 385.

Research output: Contribution to journal › Article › peer-review

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Steiner RA, Frerichs-Deeken U, Fetzner S. Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily. Acta Crystallographica Section F-Structural Biology And Crystallization Communications. 2007 Apr 28;63(5):382 - 385. gj5017. doi: 10.1107/S174430910701353X