The pecan seed storage protein vicilin, a putative food allergen, was recombinantly expressed for and purified by a combination of metal affinity and gel filtration chromatography. The protein was crystallized and studied by crystallography. The obtained crystals belonged to space group P212121 with six molecules in an asymmetric unit. The best crystal diffracted to 2.65 � resolution. The full protein did not formed crystals under screening conditions. The structure of this potential allergen was solved by molecular replacement. The refined structure gave R/Rfree values of 0.22/0.28 for all data to 2.65 �. The structural similarities and the copper binding properties of a subset of the vicilin seed storage proteins are discussed.

Purification and characterization pecan (Carya Illinoinensis) vicilin, a putative food allergen

248th National Meeting (2014)

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