Crystallization and preliminary structure determination of the plant food allergen Pru av 2.
Thaumatin-like proteins (TLPs) have mostly been investigated in the context of their function as pathogenesis-related proteins and only in recent years have some of them been classified as allergens. Here, the purification and crystallization of the first allergenic TLP, Pru av 2, a 23.3 kDa protein isolated from ripe cherries, is reported. The crystals diffracted to 2.1 A resolution at a rotating-anode generator and were found to belong to space group P2(1), with unit-cell parameters a = 44.48, b = 41.04, c = 59.16 A, beta = 106.61 degrees and one molecule per asymmetric unit. In order to obtain high-resolution data, an annealing protocol was applied that improved the resolution limit from 1.6 to 1.3 A at a synchrotron.
Dall'Antonia
Yuliya
Y
Institute of Chemistry, Structural Biology, Karl-Franzens-University Graz, Heinrichstrasse 28, 8010 Graz, Austria.
Pavkov
Tea
T
Fuchs
Heidemarie
H
Breiteneder
Heimo
H
Keller
Walter
W
D000485:Allergens / Q000737:chemistry* / Q000302:isolation & purification; D052179:Antigens, Plant / Q000737:chemistry*; D018360:Crystallography, X-Ray; D027861:Prunus; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D000485:Allergens; D052179:Antigens, Plant; C510168:Pru av 2 allergen, Prunus avium