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Characterization crystallization and preliminary X-­ray analysis of the adhesive domain of SdrE from Staphylococcus aureus

机译:金黄色葡萄球菌SdrE黏附域的表征结晶和初步X射线分析

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摘要

The adhesive domain of SdrE from Staphylococcus aureus was recombinantly expressed in Escherichia coli. The purified protein was identified by SDS–PAGE and MALDI–TOF MS. The protein was crystallized using the vapour-diffusion method in hanging-drop mode with PEG 8000 as the primary precipitating agent. X-ray diffraction data were collected to 1.8 Å resolution from a single crystal of the protein. Preliminary X-ray analysis indicated that the crystal belonged to space group P1, with unit-cell parameters a = 40.714, b = 66.355, c = 80.827 Å, α = 111.19, β = 93.99, γ = 104.39°.
机译:来自金黄色葡萄球菌的SdrE的粘附结构域在大肠杆菌中重组表达。通过SDS-PAGE和MALDI-TOF MS鉴定纯化的蛋白质。使用蒸汽扩散法以PEG 8000作为主要沉淀剂,以悬滴模式将蛋白质结晶。 X射线衍射数据是从蛋白质的单晶中以1.8Å的分辨率收集的。初步的X射线分析表明该晶体属于空间群P1,其晶胞参数a = 40.714,b = 66.355,c = 80.827,α= 111.19,β= 93.99,γ= 104.39°。

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