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Crystallization and crystallographic studies of kallistatin
Author(s) -
Lin Fang,
Zhou Aiwu,
Wei Zhenquan
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15012893
Subject(s) - crystallization , serine protease , recombinant dna , kallikrein , chemistry , crystallography , serpin , protease , biochemistry , enzyme , organic chemistry , gene
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 P 6 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.