Download MendeleyPurification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto
Yanagisawa, Y., Chatake, T., Chiba-Kamoshida, K., Naito, S., Ohsugi, T., Sumi, H., Yasuda, I., Morimoto, Y.(2010) Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 1670-1673
- PubMed: 21139221
- DOI: https://doi.org/10.1107/S1744309110043137
- Primary Citation of Related Structures:
4DWW - PubMed Abstract:
Nattokinase is a single polypeptide chain composed of 275 amino acids (molecular weight 27,724) which displays strong fibrinolytic activity. Moreover, it can activate other fibrinolytic enzymes such as pro-urokinase and tissue plasminogen activator. In the present study, native nattokinase from Bacillus subtilis natto was purified using gel-filtration chromatography and crystallized to give needle-like crystals which could be used for X-ray diffraction experiments. The crystals belonged to space group C2, with unit-cell parameters a=74.3, b=49.9, c=56.3 Å, β=95.2°. Diffraction images were processed to a resolution of 1.74 Å with an Rmerge of 5.2% (15.3% in the highest resolution shell) and a completeness of 69.8% (30.0% in the highest resolution shell). This study reports the first X-ray diffraction analysis of nattokinase.
Organizational Affiliation:
Faculty of Pharmaceutical Sciences, Chiba Institute of Science, 15-8 Shiomi-cho, Choshi, Chiba 288-0025, Japan.
