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• W2413885188 abstract "The Mannose-binding β-Prism Colocasia esculenta lectin (β-PCL) was purified from tubers using ion exchange chromatography. The purified β-PCL appeared as a single band of ∼12 kDa on SDS–PAGE. β-PCL crystallizes in trigonal space group P3121 and diffracted to a resolution of 2.1 Å. The structure was solved using Molecular replacement using Crocus vernus lectin (PDB: 3MEZ) as a model. From the final refined model to an R-factor of 16.5% and an Rfree of 20.4%, it has been observed that the biological unit consists of two β-Prism domains augmented through C-terminals swap over to form one of faces for each domain. Cα superposition of individual domains of β-PCL with individual domains of other related structures and superposition of whole protein structures were carried out. The higher RMS deviation for the superposition of whole structures suggest that β-prism domains assume different orientation in each structure." @default.
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• W2413885188 date "2016-10-01" @default.
• W2413885188 modified "2023-09-27" @default.
• W2413885188 title "Structural analysis of β-prism lectin from Colocasia esculenta (L.) S chott" @default.
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• W2413885188 doi "https://doi.org/10.1016/j.ijbiomac.2016.05.048" @default.
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