ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary crystallographic analysis of the cell-surface alginate-binding protein Algp7 isolated from Sphingomonas sp. A1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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- Crystal structure and metal binding properties of the periplasmic iron component EfeM from Pseudomonas syringae EfeUOB/M iron-transport system.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
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6 authors at 1 institution in 1 country.
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Abstract
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 P2(1)2(1)2(1), with unit-cell parameters a = 50.1, b = 98.0, c = 100.1 A, and that it diffracted to 2.8 A resolution.
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