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  • Title: Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: a cofactor-devoid dioxygenase of the alpha/beta-hydrolase-fold superfamily.
    Author: Steiner RA, Frerichs-Deeken U, Fetzner S.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2007 May 01; 63(Pt 5):382-5. PubMed ID: 17565176.
    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 His6-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 A 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 A.
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