Open AccessExpression, purification, crystallization and preliminary X‐ray diffraction analysis of Sagittaria sagittifolia arrowhead protease inhibitor API‐A in complex with bovine trypsin
Author(s) -
Jiang Chunhui,
Bao Rui,
Chen Yuxing
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108032454
Subject(s) - protease , serine protease , trypsin , proteases , crystallization , protease inhibitor (pharmacology) , biochemistry , chemistry , biology , enzyme , microbiology and biotechnology , virology , organic chemistry , virus , antiretroviral therapy , viral load
Protease inhibitors play key roles in physiological processes. Arrowhead protease inhibitor A (API‐A), a member of the serine protease inhibitor family, can inhibit two trypsin molecules simultaneously. In the present work, API‐A from Sagittaria sagittifolia has been cloned, expressed, purified and crystallized in complex with bovine trypsin. The crystals were obtained by the sitting‐drop method. A data set was collected to 2.48 Å resolution from a single crystal. The crystal belonged to space group C 222 1 , with unit‐cell parameters a = 76.63, b = 110.86, c = 152.99 Å, α = β = γ = 90°.