Crystallization and crystallographic studies of kallistatin

Journal Article · Tue Aug 25 04:00:00 EDT 2015 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X15012893· OSTI ID:22420139

Lin, Fang; Zhou, Aiwu; Wei, Zhenquan ^[1]

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1. Shanghai Jiaotong University School of Medicine (Room 1006, Building 2, No 280, South Chongqing Road), Shanghai 200025, People’s Republic of (China)

The crystallization of human kallistatin in the relaxed conformation is reported. 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 P6{sub 1}, 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 β-sheet.

• OSTI ID: 22420139
• Journal Information: Acta Crystallographica. Section F, Structural Biology Communications, Journal Name: Acta Crystallographica. Section F, Structural Biology Communications Journal Issue: Pt 9 Vol. 71; ISSN ACSFEN; ISSN 2053-230X
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
ANIMAL TISSUES
CRYSTALLIZATION
ESCHERICHIA COLI
HEXAGONAL LATTICES
SPACE GROUPS
X-RAY DIFFRACTION