Steiner Roberto A, Frerichs-Deeken Ursula, Fetzner Susanne
Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):382-5. doi: 10.1107/S174430910701353X. Epub 2007 Apr 6.
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.
1H-3-羟基-4-氧代喹哪啶2,4-双加氧酶(HOD)是一种不含辅因子的双加氧酶,参与喹哪啶降解的邻氨基苯甲酸途径。有人提出HOD属于α/β-水解酶折叠超家族的酶。N端带有His6标签的HOD已通过悬滴气相扩散法结晶,使用酒石酸钠/钾作为沉淀剂,CuCl2作为添加剂。该结构通过在Cu吸收峰波长下收集到3.5埃分辨率的数据,采用单波长反常散射(SAD)技术解析。晶体属于原始四方空间群P4(3)2(1)2,晶胞参数a = b = 153.788,c = 120.872埃。