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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1647-51. doi: 10.1107/S1744309110042272. Epub 2010 Nov 26.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, Affinity
  • Chromatography, Gel
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Galectins / chemistry*
  • Humans
  • Lactose / chemistry
  • Zebrafish / metabolism*
  • Zebrafish Proteins / chemistry*


  • Gal1-L2 protein, zebrafish
  • Galectins
  • Zebrafish Proteins
  • Lactose