首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Cloning expression purification and preliminary X-­ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thaliana
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Cloning expression purification and preliminary X-­ray analysis of the protein kinase domain of constitutive triple response 1 (CTR1) from Arabidopsis thaliana

机译:拟南芥组成型三联反应1(CTR1)蛋白激酶结构域的克隆表达纯化和X射线初步分析

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摘要

Ethylene, a gaseous plant hormone, is perceived by a group of membrane-bound receptors. Constitutive triple response 1 (CTR1) from Arabidopsis thaliana directly interacts with ethylene receptors and thus links signal reception to the intracellular signalling pathway. The C-terminal protein kinase domain of CTR1 has been crystallized in its wild-type form and as a kinase-dead mutant. The wild-type crystals diffracted X-ray radiation to 3 Å resolution and the crystals of the kinase-dead mutant diffacted to 2.5 Å resolution. The crystals belonged to space groups P41212 and P42212, respectively, with two molecules per asymmetric unit in both cases.
机译:乙烯是一种气态植物激素,可被一组膜结合受体感知。拟南芥的本构三联反应1(CTR1)直接与乙烯受体相互作用,因此将信号接收链接到细胞内信号通路。 CTR1的C末端蛋白激酶结构域已经以其野生型形式和作为激酶死亡的突变体进行了结晶。野生型晶体将X射线辐射衍射至3Å分辨率,而激酶死亡突变体的晶体衍射至2.5Å分辨率。两种晶体分别属于P41212和P42212空间群,每个不对称单元有两个分子。

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