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Purification, identification and preliminary crystallographic studies of an allergenic protein from Solanum melongena
Author(s) -
Jain Abha,
Salunke Dinakar Masanu
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000734
Subject(s) - melongena , solanum , identification (biology) , botany , crystallography , biology , chemistry
Solanum melongena (eggplant), a member of the Solanaceae family, is a widely cultivated vegetable crop and is commonly used as a food throughout the world. Allergic reactions caused by members of this family are well known. However, mechanistic analyses to understand their molecular basis have not been adequately explored. In order to address this issue, the 7S vicilin protein (SM80.1) of size 45 kDa was purified from seeds of S. melongena by ammonium sulfate fractionation and size‐exclusion chromatography. Significant homology of SM80.1 to an allergy‐related protein from S. lycopersicum was identified through a BLAST search. Crystallization attempts with purified protein using the hanging‐drop vapour‐diffusion method led to hexagonal‐shaped crystals. The crystals diffracted to 2.21 Å resolution and belonged to space group P 6 3 22, with unit‐cell parameters a = 117.9, c = 123.5 Å.