Ferritin is a class of proteins ubiquitously found in various types of nucleated organisms and involved in the ironhomeostasis regulation of body. Ferritin can self-assemble to form a hollow nanocage of about 14 nm in size and is often usedas carrier for drug delivery and vaccine construction. The crystal structure of Mycoplasma ferritin shows atypical ferroxidasecentres and new pathway for Fe2+ uptake, which are structurally different from those of other species. Not much work has beenreported for Spiroplasma ferritin. Here, our studies show that Spiroplasma ferritin has low sequence similarity with other ferri tins including Mycoplasma ferritins. Spiroplasma eriocheiris Ferritin (SeFer) was recombinant expressed in E. coli in solubleform after IPTG (isopropyl-beta-D-thiogalactopyranoside) induction. High-purity SeFer protein was obtained after purificationby DEAE (diethylaminoethyl) weak anion exchange chromatography and gel filtration. Crystal screen of SeFer was performedby sitting drop vapor diffusion at 4℃ and 18℃. SeFer crystals grew in several screen conditions. The best crystal diffracted to2.90 ? by synchrotron radiation source and it belonged to the I432 space group. The X-ray crystallography data collected herecan be used for further structure determination. Native-PAGE, dynamic light scattering, and the position of peaks of SeFer inmolecular sieve showed that the molecular weight of SeFer is about 400.0 kD, and the diameter of SeFer was about 15 nm, bothof them are close to the theoretical value. The structural model of SeFer was predicted by using Alphafold 2. The predicted mod el shows that SeFer has a regular icosahedral overall structure, which is similar to other ferritins. However, SeFer model showsthat the key residues of ferroxidase center differ from those of mycoplasma ferritin. Our results not only provide a basis forstudying the crystal structure of SeFer, but also provide new candidates for vaccine vectors.