Crystallization and preliminary X-ray crystallographic analysis of zebrafish prototype galectin Drgal1-L2

Abstract

Zebrafish (Danio rerio) are an important developmental and embryological model given the optical clarity of embryos and larvae that permit 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 that is a carbohydrate-binding protein exhibiting β-galactoside binding specificity and which is over-expressed by many aggressive human cancers. This study describes the cloning, expression in Escherichia coli, purification and crystallisation 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 characterisation.