Article

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

Faculty of Pharmaceutical Sciences, Chiba Institute of Science, 15-8 Shiomi-cho, Choshi, Chiba 288-0025, Japan.
Acta Crystallographica Section F Structural Biology and Crystallization Communications (impact factor: 0.51). 12/2010; 66(Pt 12):1670-3. DOI:10.1107/S1744309110043137 pp.1670-3
Source: 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.

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Keywords

displays strong fibrinolytic activity
 
fibrinolytic enzymes
 
first X-ray diffraction analysis
 
native nattokinase
 
pro-urokinase
 
space group C2
 
tissue plasminogen activator
 
X-ray diffraction experiments