新型 S-腺苷-L-蛋氨酸依赖型 C-甲基转移酶 CouO 的结晶和初步衍射数据分析。

IF 0.9 4区生物学

Acta Crystallographica Section F-structural Biology and Crystallization Communications Pub Date : 2012-06-01 Epub Date: 2012-05-23 DOI:10.1107/S1744309112017137

Andrzej Lyskowski, Martin Tengg, Georg Steinkellner, Helmut Schwab, Mandana Gruber-Khadjawi, Karl Gruber

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引用次数: 0

摘要

我们成功地克隆、表达和纯化了来自利尻链霉菌（Streptomyces rishiriensis）的重组 Q9F8T9 蛋白（CouO），它是一种依赖于 S-腺苷-L-蛋氨酸的 C-甲基转移酶。CouO 是在 Morpheus 结晶筛选的单一条件下结晶的。玻璃化晶体的衍射分辨率为 2.05 Å，属于空间群 P2(1)，单位晶胞参数 a = 33.02，b = 82.87，c = 76.77 Å，β = 96.93°。

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Crystallization of the novel S-adenosyl-L-methionine-dependent C-methyltransferase CouO from Streptomyces rishiriensis and preliminary diffraction data analysis.

Recombinant Q9F8T9 protein from Streptomyces rishiriensis (CouO), an S-adenosyl-L-methionine-dependent C-methyltransferase, has been successfully cloned, expressed and purified. CouO was crystallized from a single condition in the Morpheus crystallization screen. A vitrified crystal diffracted to 2.05 Å resolution and belonged to space group P2(1), with unit-cell parameters a = 33.02, b = 82.87, c = 76.77 Å, β = 96.93°.

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来源期刊

Acta Crystallographica Section F-structural Biology and Crystallization Communications 生物-晶体学

自引率

0.00%

发文量

审稿时长

2-4 weeks

期刊介绍： Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.