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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, purification and preliminary X-ray analysis of a fibrillarin homolog from Methanococcus jannaschii, a hyperthermophile.
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Expression, purification and preliminary X-ray analysis of a fibrillarin homolog from Methanococcus jannaschii, a hyperthermophile.

机译:表达、纯化和初步的x射线分析fibrillarin同族体产甲烷球菌属jannaschii超嗜热菌。

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摘要

Fibrillarin plays a central role in ribosome biogenesis as a ribosomal RNA-processing protein. A Methanococcus jannaschii homolog of fibrillarin has been overexpressed, purified and crystallized. Crystals belong to the C2 space group with unit-cell parameters a = 121.4, b = 43.2, c = 55.3 A, beta = 96.9 degrees. Under flash-frozen conditions and using synchrotron radiation, the crystals diffract to 1.8 A resolution. For structural determination, a selenomethionine derivative of the protein has also been crystallized.
机译:Fibrillarin核糖体中起着重要的作用生物起源的核糖体rna加工蛋白质。一个产甲烷球菌属jannaschii fibrillarin同族体过表达,纯化,结晶。b组与晶胞参数= 121.4,=43.2, c = 55.3,β= 96.9度。瞬间冷冻条件和使用同步加速器辐射,1.8的晶体衍射决议。硒代蛋氨酸导数的蛋白质结晶。

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