首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Expression purification crystallization and preliminary X-ray analysis of the polysaccharide lyase RB5312 from the marine planctomycete Rhodopirellula baltica
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Expression purification crystallization and preliminary X-ray analysis of the polysaccharide lyase RB5312 from the marine planctomycete Rhodopirellula baltica

机译:海洋浮游细菌波氏假单胞菌多糖裂解酶RB5312的表达纯化结晶和初步X射线分析

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摘要

Polysaccharide lyases belonging to family PL1 act on pectins. These anionic polymers are usually produced by terrestrial plants and therefore pectinolytic enzymes are not frequently observed in marine microorganisms. The protein RB5312 from the marine bacterium Rhodopirellula baltica is distantly related to family PL1 pectate lyases, but its exact function is unclear. In this study, the expression and purification of a recombinant form of RB5312 are described. This protein was crystallized using the hanging-drop vapour-diffusion method. The crystals belongs to space group P212121, with unit-cell parameters a = 39.05, b = 144.05, c = 153.97 Å, α = β = γ = 90°. A complete data set was collected to 1.8 Å resolution from a native crystal.
机译:属于PL1家族的多糖裂解酶作用于果胶上。这些阴离子聚合物通常由陆生植物生产,因此在海洋微生物中不经常观察到果胶分解酶。来自海洋细菌波多黎各红假单胞菌的蛋白RB5312与PL1果胶酸家庭裂解酶有很远的联系,但其确切功能尚不清楚。在这项研究中,描述了重组形式的RB5312的表达和纯化。使用悬滴蒸气扩散法使该蛋白质结晶。晶体属于空间群P212121,单位晶胞参数a = 39.05,b = 144.05,c = 153.97Å,α=β=γ= 90°。从天然晶体收集了一个完整的数据集,分辨率为1.8Å。

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