ArticleActa crystallographica. Section F, Structural biology communications2015
Purification, identification and preliminary crystallographic studies of an allergenic protein from Solanum melongena.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Review
- Crystal structure of the vicilin from Solanum melongena reveals existence of different anionic ligands in structurally similar pockets.Scientific reports · 2016Article
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2 authors.
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Abstract
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 P6322, with unit-cell parameters a = 117.9, c = 123.5 Å.
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