Open AccessProtein preparation, crystallization and preliminary X‐ray analysis of Polygonum cuspidatum bifunctional chalcone synthase/benzalacetone synthase
Author(s) -
Lu Heshu,
Yang Mingfeng,
Liu Chunmei,
Lu Ping,
Cang Huaixing,
Ma Lanqing
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113017004
Subject(s) - atp synthase , chemistry , chalcone synthase , chalcone , biochemistry , enzyme , stereochemistry , biosynthesis
The chalcone synthase (CHS) superfamily of type III polyketide synthases (PKSs) generate the backbones of a variety of plant secondary metabolites. An active bifunctional chalcone synthase/benzalacetone synthase (CHS/BAS) from Polygonum cuspidatum was overexpressed in Escherichia coli as a C‐terminally polyhistidine‐tagged fusion protein, purified to homogeneity and crystallized using polyethylene glycol 4000 as a precipitant. The production of well shaped crystals of the complex between PcPKS1 and benzalacetone was dependent on the presence of sorbitol and barium chloride as additives. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 80.23, b = 81.01, c = 122.89 Å, and diffracted X‐rays to at least 2.0 Å resolution.