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Morphology of the ferritin iron core by aberration corrected scanning transmission electron microscopy

机译：通过像差校正的扫描透射电子显微镜观察铁蛋白铁心的形貌

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摘要

As the major iron storage protein, ferritin stores and releases iron for maintaining the balance of iron in fauna, flora, and bacteria. We present an investigation of the morphology and iron loading of ferritin (from equine spleen) using aberration-corrected high angle annular dark field scanning transmission electron microscopy. Atom counting method, with size selected Au clusters as mass standards, was employed to determine the number of iron atoms in the nanoparticle core of each ferritin protein. Quantitative analysis shows that the nuclearity of iron atoms in the mineral core varies from a few hundred iron atoms to around 5000 atoms. Moreover, a relationship between the iron loading and iron core morphology is established, in which mineral core nucleates from a single nanoparticle, then grows along the protein shell before finally forming either a solid or hollow core structure.
机译：铁蛋白作为主要的铁存储蛋白，可以存储和释放铁，以保持动物，植物和细菌中铁的平衡。我们目前使用像差校正的高角度环形暗场扫描透射电子显微镜对铁蛋白（来自马脾）的形态和铁负荷的研究。原子计数法以大小选定的金簇为质量标准，用于确定每种铁蛋白蛋白质的纳米颗粒核心中的铁原子数。定量分析表明，矿物核心中铁原子的核数从几百个铁原子到约5000个原子不等。此外，建立了铁负载和铁核形态之间的关系，其中矿物核从单个纳米颗粒成核，然后沿着蛋白质壳生长，最终形成实心或空心核结构。

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