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Crystallization and crystallographic studies of kallistatin.

ABSTRACT: Kallistatin is a serine protease inhibitor (serpin) which specifically inhibits human tissue kallikrein; however, its inhibitory activity is inhibited by heparin. In order to elucidate the underlying mechanism, recombinant human kallistatin was prepared in Escherichia coli and the protein was crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.9?Å resolution. The crystals were found to belong to space group P61, with unit-cell parameters a = 113.51, b = 113.51, c = 76.17?Å. Initial analysis indicated that the crystallized kallistatin was in a relaxed conformation, with its reactive-centre loop inserted in the central ?-sheet.

SUBMITTER: Lin F

PROVIDER: S-EPMC4555919 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Crystallization and crystallographic studies of kallistatin.

Lin Fang F Zhou Aiwu A Wei Zhenquan Z

Acta crystallographica. Section F, Structural biology communications 20150825 Pt 9

Kallistatin is a serine protease inhibitor (serpin) which specifically inhibits human tissue kallikrein; however, its inhibitory activity is inhibited by heparin. In order to elucidate the underlying mechanism, recombinant human kallistatin was prepared in Escherichia coli and the protein was crystallized by the sitting-drop vapour-diffusion method. X-ray diffraction data were collected to 1.9 Å resolution. The crystals were found to belong to space group P61, with unit-cell parameters a = 113.5 ...[more]

PMID: 26323298

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