Abstract
Staphylokinase, a fibrin-specific plasminogen activator, was highly expressed in Escherichia coli and purified by ion-exchange and gel-filtration chromatography. The purified recombinant staphylokinase was fully active and readily crystallized against 1.2 M sodium citrate in 100mM Tris-HCl buffer at pH8.0 using the hanging-drop method. Crystals of staphylokinase diffract to better than 2.2 Å resolution. The crystal belongs to the tetragonal space group P41212 or its enantiomorph with unit-cell parameters a = b = 67.5, c = 150.1 Å. There are two molecules in the asymmetric unit. In this paper, we described the first crystallization of a kind of plasminogen activator and present the results of preliminary X-ray diffraction data from the native protein.
Original language | English (US) |
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Pages (from-to) | 564-565 |
Number of pages | 2 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 52 |
Issue number | 3 |
State | Published - May 1 1996 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Clinical Biochemistry
- Structural Biology
- Condensed Matter Physics