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.
Institute for Glycomics, Griffith University (Gold Coast Campus), Queensland 4222, Australia.
Stacy A
SA
Scott
Matthew O
MO
Cozier
Pauline D I
PD
Dubar
Manasa
M
Ramakrishna
Ken
K
Scott
Helen
H
Blanchard
D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D037161:Galectins / Q000737:chemistry*; D006801:Humans; D007785:Lactose / Q000737:chemistry; D015027:Zebrafish / Q000378:metabolism*; D029961:Zebrafish Proteins / Q000737:chemistry*
C541498:Gal1-L2 protein, zebrafish; D037161:Galectins; D029961:Zebrafish Proteins; D007785:Lactose