Binding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures

Volume: 524, Issue: 1, Pages: 268 - 271
Published: Mar 1, 2020
Abstract
X-ray intensities extending to 1.4 Å resolution were collected on the P63 hexagonal crystal form of canavalin, and extended to 1.9 Å for the orthorhombic C2221 crystals. Structure determination of a new crystal form of canavalin having space group P212121 is reported as well. Both the N and C terminal cupin domains contained identifiable ligands. For hexagonal crystals, in the cavity of the C terminal cupin, a molecule of benzoic acid was found,...
Paper Details
Title
Binding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures
Published Date
Mar 1, 2020
Volume
524
Issue
1
Pages
268 - 271
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