首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary crystallographic analysis of the cell-surface alginate-binding protein Algp7 isolated from Sphingomonas sp. A1
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Crystallization and preliminary crystallographic analysis of the cell-surface alginate-binding protein Algp7 isolated from Sphingomonas sp. A1

机译:从鞘氨醇单胞菌分离的细胞表面藻酸盐结合蛋白Algp7的结晶和初步晶体学分析。 A1

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摘要

Sphingomonas sp. A1, a Gram-negative bacterium, directly internalizes alginate macromolecules through a mouth-like pit that is present on its cell surface. The alginate-binding protein Algp7, which was found to be localized on the cell surface, contributes to the accumulation of alginate in the pit. Algp7 was crystallized at 293 K by means of the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as a crystallizing agent. Preliminary X-ray analysis showed that the Algp7 crystal belonged to space group P212121, with unit-cell parameters a = 50.1, b = 98.0, c = 100.1 Å, and that it diffracted to 2.8 Å resolution.
机译:鞘氨醇单胞菌革兰氏阴性细菌A1通过其细胞表面上存在的口状凹坑直接内化藻酸盐大分子。被发现位于细胞表面的藻酸盐结合蛋白Algp7促进了藻酸盐在坑中的积累。通过坐滴蒸气扩散法,以聚乙二醇3350作为结晶剂,使Algp7在293 K下结晶。初步的X射线分析表明,Algp7晶体属于空间群P212121,单位晶胞参数a = 50.1,b = 98.0,c = 100.1Å,并且衍射到2.8Å分辨率。

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