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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein.
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Preliminary X-ray crystallographic analysis of the complex between the DNAase domain of colicin E9 and its cognate immunity protein.

机译:初步的x射线晶体分析复杂的大肠杆菌素E9 DNAase域之间的及其同源免疫蛋白。

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摘要

We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, Kd = 1 x 10(-16) M, reveals it to be one of the highest affinity protein-protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P212121 with one molecule of complex in the asymmetric unit, and crystals contain approximately 43% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.
机译:我们有结晶和初步完成x射线之间的复杂的特征DNAase域的E9大肠杆菌素及其同源免疫蛋白质Im9。对于这个复杂,Kd = 1 x 10(-16)米,揭示了它亲和力蛋白质最高的国家之一已知的相互作用。复杂的种植从microseeding实验使用挂钩4 k作为沉淀剂。P212121与一个复杂的分子不对称单位,晶体包含大约43%的溶剂。天生non-isomorphous所以selenomethionine-derivatized蛋白质已经准备和疯狂的定相晶体生长实验。

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