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里氏非血红素铁加氧酶系统咔唑1,9a -双加氧酶中铁氧化还原蛋白还原酶组分的结晶及初步X射线衍射研究。

Crystallization and preliminary X-ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a-dioxygenase.

作者信息

Ashikawa Yuji, Uchimura Hiromasa, Fujimoto Zui, Inoue Kengo, Noguchi Haruko, Yamane Hisakazu, Nojiri Hideaki

机构信息

Biotechnology Research Center, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt 6):499-502. doi: 10.1107/S174430910702163X. Epub 2007 May 12.

DOI:10.1107/S174430910702163X
PMID:17554172
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2335075/
Abstract

Carbazole 1,9a-dioxygenase (CARDO), which consists of an oxygenase component (CARDO-O) and the electron-transport components ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R), catalyzes dihydroxylation at the C1 and C9a positions of carbazole. CARDO-R was crystallized at 277 K using the hanging-drop vapour-diffusion method with the precipitant PEG 8000. Two crystal types (types I and II) were obtained. The type I crystal diffracted to a maximum resolution of 2.80 A and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 158.7, c = 81.4 A. The type II crystal was obtained in drops from which type I crystals had been removed; it diffracted to 2.60 A resolution and belonged to the same space group, with unit-cell parameters a = b = 161.8, c = 79.5 A.

摘要

咔唑1,9a -双加氧酶(CARDO)由一个加氧酶组分(CARDO - O)以及电子传递组分铁氧还蛋白(CARDO - F)和铁氧还蛋白还原酶(CARDO - R)组成,催化咔唑C1和C9a位的双羟基化反应。使用含有沉淀剂聚乙二醇8000的悬滴气相扩散法,在277 K条件下使CARDO - R结晶。获得了两种晶体类型(I型和II型)。I型晶体的衍射极限分辨率为2.80 Å,属于空间群P4(2)2(1)2,晶胞参数a = b = 158.7,c = 81.4 Å。II型晶体是从已去除I型晶体的液滴中获得的;其衍射分辨率为2.60 Å,属于同一空间群且晶胞参数a = b = 161.8,c = 79.5 Å。

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