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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic analysis of the excisionase-DNA complex from bacteriophage lambda.
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Crystallization and preliminary X-ray crystallographic analysis of the excisionase-DNA complex from bacteriophage lambda.

机译:结晶和初步的x射线晶体excisionase-DNA的分析复杂的从噬菌体λ。

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摘要

Bacteriophage lambda uses an elegantly regulated and highly directional site-specific DNA-recombination reaction to integrate and excise its genome. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which dramatically stimulates excision by orchestrating the assembly of a higher order nucleoprotein structure that excises the prophage. The Xis protein stabilizes this recombination intermediate by substantially altering the trajectory of viral DNA and by cooperatively interacting with the lambda integrase (Int) protein. In an attempt to understand how Xis controls the directionality of bacteriophage lambda recombination, co-crystals of the DNA-binding domain of Xis in complex with its binding site within the P-arm of the phage have been obtained using the hanging-drop vapor-diffusion method. Using sodium acetate as a precipitating reagent, the Xis-DNA complex crystallizes in space group C2, with unit-cell parameters a = 80.2, b = 72.7, c = 38.8 A, beta = 104.1 degrees. These crystals diffract beyond 1.5 A resolution and are well suited for structural analysis using X-ray crystallography.
机译:噬菌体λ使用一个优雅的监管和高度定向特定站点集成和dna重组反应切除它的基因组。过程phage-encoded切除酶(切除酶)蛋白质,这大大刺激切除通过编排组装的高阶核蛋白质结构,废寝忘食前噬菌体。复合中间的大幅改变病毒DNA的轨迹合作互动的λ整合酶(Int)的蛋白质。了解切除酶控制的方向噬菌体λ重组,co-crystals切除酶dna结合域的复杂其结合位点的P-arm噬菌体已获得使用悬滴吗扩散的方法。沉淀试剂,Xis-DNA复杂在空间群C2结晶,晶胞参数= 80.2,= 72.7 b, c = 38.8,β=104.1度。一项决议,非常适合结构使用x射线晶体学分析。

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