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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Expression, purification, crystallization and preliminary X-ray crystallographic studies of hepatitis B virus core fusion protein corresponding to octahedral particles
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Expression, purification, crystallization and preliminary X-ray crystallographic studies of hepatitis B virus core fusion protein corresponding to octahedral particles

机译:八面体颗粒对应的乙型肝炎病毒核心融合蛋白的表达,纯化,结晶和初步X射线晶体学研究

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摘要

Recombinant hepatitis B virus core proteins dimerize to form building blocks that are capable of self-assembly into a capsid. A core capsid protein dimer (CPD) linked to a green fluorescent protein variant, EGFP, at the C-terminus has been designed. The recombinant fusion CPD was expressed in Escherichia coli, assembled into virus-like particles (VLPs), purified and crystallized. The single crystal diffracted to 2.15 angstrom resolution and belonged to the cubic space group F432, with unit-cell parameters a = b = c = 219.7 angstrom. The fusion proteins assembled into icosahedral VLPs in aqueous solution, but were rearranged into octahedral symmetry through the crystal-packing process under the crystallization conditions.
机译:重组乙型肝炎病毒核心蛋白二聚形成可自我组装成衣壳的构件。已经设计了在C末端连接绿色荧光蛋白变体EGFP的核心衣壳蛋白二聚体(CPD)。重组融合CPD在大肠杆菌中表达,组装成病毒样颗粒(VLP),纯化并结晶。单晶衍射到2.15埃的分辨率,属于立方空间群F432,单位晶胞参数a = b = c = 219.7埃。融合蛋白在水溶液中组装成二十面体VLP,但在结晶条件下通过晶体堆积过程重新排列为八面体对称性。

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