skip to main content

Title: Crystallization and crystallographic studies of kallistatin

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.
Authors:
; ;  [1]
  1. Shanghai Jiaotong University School of Medicine (Room 1006, Building 2, No 280, South Chongqing Road), Shanghai 200025, People’s Republic of (China)
Publication Date:
OSTI Identifier:
22420139
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F, Structural Biology Communications; Journal Volume: 71; Journal Issue: Pt 9; Other Information: PMCID: PMC4555919; PMID: 26323298; PUBLISHER-ID: hc5193; PUBLISHER-ID: S2053230X15012893; OAI: oai:pubmedcentral.nih.gov:4555919; Copyright (c) Lin et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ANIMAL TISSUES; CRYSTALLIZATION; ESCHERICHIA COLI; HEXAGONAL LATTICES; SPACE GROUPS; X-RAY DIFFRACTION