The presence of thiosulfate in the protein solution was essential to promote crystal growth and to avoid the formation of unstable and weakly diffracting crystals(1); this is likely to be a consequence of the intrinsic capability of the reduced thiol group of the active-site cysteine to form disulfide bridges, leading to the destabilization of the protein native structure. Sulfane sulfur-donor compounds such as Na2S2O3 are likely to either keep the protein in the persulfurated form or to prevent intermolecular disulfide bridges leading to unfolding and aggregation

硫代硫酸钠防止分子间二硫键
蛋白质溶液中硫代硫酸盐的存在对于促进晶体生长和避免形成不稳定和弱衍射晶体至关重要 (1)；这可能是活性位点半胱氨酸的还原硫醇基团形成二硫键的内在能力的结果，导致蛋白质天然结构的不稳定。硫烷硫供体化合物（如 Na2S2O3）可能使蛋白质保持过硫化形式或防止分子间二硫键导致展开和聚集 。

(2). References 参考文献

1. Crystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major. D. Bisacchi, Y. Zhou, B. P. Rosen, R. Mukhopadhyay and D. Bordo. Acta Cryst. (2006). F62, 976-979. 2. Bordo, D., Forlani, F., Spallarossa, A., Colnaghi, R., Carpen, A., Bolognesi, M. & Pagani, S. (2001). Biol. Chem. 382, 1245–1252.