Purification, crystallization and preliminary X‐ray diffraction experiment of nattokinase from Bacillus subtilis natto
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 R merge 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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