首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Cloning purification crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae
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Cloning purification crystallization and preliminary X-ray diffraction crystallographic study of acyl-protein thioesterase 1 from Saccharomyces cerevisiae

机译:酿酒酵母酰基蛋白硫酯酶1的克隆纯化结晶及初步X射线衍射晶体学研究

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摘要

Palmitoylation/depalmitoylation plays an important role in protein modification. yApt1 is the only enzyme in Saccharomyces cerevisiae that catalyses depalmitoylation. In the present study, recombinant full-length yApt1 was cloned, expressed, purified and crystallized. The crystals diffracted to 2.40 Å resolution and belonged to space group P42212, with unit-cell parameters a = b = 146.43, c = 93.29 Å. A preliminary model of the three-dimensional structure has been built and further refinement is ongoing.
机译:棕榈酰化/去棕榈酰化在蛋白质修饰中起重要作用。 yApt1是酿酒酵母中唯一能催化去棕榈酸酯化的酶。在本研究中,重组全长yApt1被克隆,表达,纯化和结晶。晶体衍射至2.40Å分辨率,属于P42212空间群,单位晶格参数a = b = 146.43,c = 93.29Å。已经建立了三维结构的初步模型,并且正在进行进一步的改进。

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