Crystallization and preliminary X-ray diffraction studies of recombinant staphylokinase

Chunhui Zhan, Zhuli Wan, Wenrui Chang, Junjie Yue, Dongcai Liang, Qiqun Tang, Yinliang Gu, Xiaoxuan Zhang, Guang Xu, Yunsong Zhu, Houyan Song

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


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 languageEnglish (US)
Pages (from-to)564-565
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Issue number3
StatePublished - May 1 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Clinical Biochemistry
  • Structural Biology
  • Condensed Matter Physics


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