|LEE, BORAM - Korean Advanced Institute Of Science And Technology (KAIST)|
Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 5/8/2014
Publication Date: 8/13/2014
Citation: Zhang, Y., Lee, B., Du, W., Grauke, L.J., McHugh, T.H. 2014. Purification and characterization pecan (Carya Illinoinensis) vicilin, a putative food allergen (abstract). Meeting abstract presented at the American Chemical Society National Meeting on August 13, 2014.
Technical Abstract: 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 Å 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 Å. The structural similarities and the copper binding properties of a subset of the vicilin seed storage proteins are discussed.