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  • Title: Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus.
    Author: Qureshi IA, Sethi DK, Salunke DM.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2006 Sep 01; 62(Pt 9):869-72. PubMed ID: 16946466.
    Abstract:
    A 24 kDa protein was purified from the seeds of Lathyrus sativus by ammonium sulfate fractionation and ion-exchange chromatography. The N-terminal amino-acid sequence showed significant homology with the 2S albumin class of seed storage proteins. The protein showed 85% sequence homology with the seed albumin of Pisum sativum within the 40 N-terminal residues. Crystals were obtained by the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 43.5, b = 82.7, c = 153.4 A.
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