Crystallization and preliminary X-ray diffraction studies of recombinant staphylokinase.
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 100 mM Tris-HCl buffer at pH 8.0 using the hanging-drop method. Crystals of staphylokinase diffract to better than 2.2 A resolution. The crystal belongs to the tetragonal space group P4(1)2(1)2 or its enantiomorph with unit-cell parameters a = b = 67.5, c = 150.1 A. 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.
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
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Zhan
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Wan
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Chang
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J
Yue
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D
Liang
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Tang
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Gu
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Zhang
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Xu
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Zhu
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Song