Crystallization and preliminary X‐ray crystallographic analysis of zebrafish prototype galectin Drgal1‐L2
Zebrafish (Danio rerio) are an important developmental and embryological model given the optical clarity of the embryos and larvae, which permits real‐time viewing of developing pathologies. More recently, a broader scope for these vertebrates to model a range of human diseases, including some cancers, has been indicated. Zebrafish Drgal1‐L2 has been identified as an orthologue of mammalian galectin‐1, which is is a carbohydrate‐binding protein that exhibits β‐galactoside‐binding specificity and which is overexpressed by many aggressive human cancers. This study describes the cloning, expression in Escherichia coli, purification and crystallization of recombinant Drgal1‐L2 protein in the presence of lactose (ligand). X‐ray diffraction data from these novel crystals of zebrafish Drgal1‐L2 were collected to a resolution of 1.5 Å using a synchrotron‐radiation source, enabling their characterization.
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