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Expression, purification and crystallization of pecan ( Carya illinoinensis ) vicilin
Author(s) -
Lee BoRam,
Zhang Renhao,
Du WenXian,
Grauke Larry J.,
McHugh Tara H.,
Zhang YuZhu
Publication year - 2014
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/s2053230x14012369
Subject(s) - vicilin , isoprene , biology , botany , storage protein , chemistry , food science , biochemistry , organic chemistry , gene , copolymer , polymer
Tree nuts are responsible for many cases of severe food allergies. The 7S seed storage protein vicilin has been identified as a food allergen in many kinds of tree nuts. The vicilin protein consists of an N‐terminal low‐complexity region with antimicrobial activity and a C‐terminal domain that forms a trimeric structure that belongs to the cupin superfamily. In this study, vicilin from pecan ( Carya illinoinensis ) was isolated and was expressed in bacteria for the first time. The cupin structural core of the protein, residues 369–792, was purified by metal‐affinity and gel‐filtration chromatography to high purity. Vicilin crystals were obtained and the best crystal diffracted to 2.65 Å resolution in space group P 2 1 2 1 2 1 .