Open AccessCrystallization and preliminary crystallographic characterization of the N‐terminal Kunitz domain of boophilin
Author(s) -
Cereija Tatiana B.,
Figueiredo Ana C.,
de Sanctis Daniele,
Tanaka Aparecida S.,
Pereira Pedro José Barbosa
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112005532
Subject(s) - crystallization , crystallography , orthorhombic crystal system , serine protease , resolution (logic) , thrombin , trypsin , chemistry , materials science , crystal structure , biochemistry , protease , enzyme , biology , organic chemistry , computer science , platelet , artificial intelligence , immunology
Boophilin is a tight‐binding thrombin inhibitor composed of two canonical Kunitz‐type domains in a tandem arrangement. Thrombin‐bound boophilin can inhibit a second trypsin‐like serine proteinase, most likely through the reactive loop of its N‐terminal Kunitz domain. Here, the crystallization and preliminary crystallographic analysis of the isolated N‐terminal domain of boophilin is reported. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 and diffracted to beyond 1.8 Å resolution using a sealed‐tube home source and to 0.87 Å resolution at a synchrotron source.