Crystallization and preliminary structure determination of the plant food allergen Pru av 2

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Yuliya Dall'AntoniaWalter Keller

Abstract

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.

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Citations

Aug 6, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Pankaj GuptaDinakar M Salunke
Feb 18, 2011·BMC Plant Biology·Benjamin PetreSébastien Duplessis
Feb 25, 2010·Genome Biology·Nicole M GerardoAndreas Vilcinskas
Mar 20, 2012·Molecular Immunology·C Shi, J D Miller
May 3, 2018·Probiotics and Antimicrobial Proteins·Jian LiuYawei Shi
Sep 22, 2020·Bioinformatics and Biology Insights·Carlos André Dos Santos-SilvaAna Maria Benko-Iseppon
Jan 21, 2012·Journal of Agricultural and Food Chemistry·Joana CostaMaria Beatriz P P Oliveira

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