Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto.

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, ?=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.

SUBMITTER: Yanagisawa Y 

PROVIDER: S-EPMC2998380 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature