Purification, crystallization and initial crystallographic characterization of peanut major allergen Ara h 3.
The peanut is a significant food source, but is responsible for many cases of anaphylaxis. The peanut 11S legumin-like seed storage protein Ara h 3 is one of the best characterized allergens. In this study, Ara h 3 was extracted from peanut kernels and purified by sequential anion-exchange, hydrophobic interaction and gel-filtration chromatography to very high purity to facilitate crystallization and structural studies. Well diffracting single crystals were obtained by the vapor-diffusion method. A molecular-replacement structural solution has been obtained and refinement of the structure is currently under way.
Jin
Tengchuan
T
Department of Biology, Illinois Institute of Technology, Chicago, IL 60616, USA.
Howard
Andrew
A
Zhang
Yu-Zhu
YZ
D000485:Allergens / Q000737:chemistry* / Q000302:isolation & purification*; D052179:Antigens, Plant; D010367:Arachis / Q000737:chemistry / Q000276:immunology*; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D010936:Plant Extracts / Q000737:chemistry; D017433:Protein Structure, Secondary; D055314:Seed Storage Proteins
D000485:Allergens; D052179:Antigens, Plant; D010936:Plant Extracts; D055314:Seed Storage Proteins; C118207:allergen Ara h3