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

Journal Article


Abstract


  • 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. © 2010 International Union of Crystallography. All rights reserved.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2010

Citation


  • Scott, S. A., Cozier, M. O., Dubar, P. D. I., Ramakrishna, M., Scott, K., & Blanchard, H. (2010). Crystallization and preliminary X-ray crystallographic analysis of zebrafish prototype galectin Drgal1-L2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(12), 1647-1651. doi:10.1107/S1744309110042272

Scopus Eid


  • 2-s2.0-78650125364

Start Page


  • 1647

End Page


  • 1651

Volume


  • 66

Issue


  • 12

Abstract


  • 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. © 2010 International Union of Crystallography. All rights reserved.

UOW Authors


  •   Blanchard, Helen (external author)

Publication Date


  • 2010

Citation


  • Scott, S. A., Cozier, M. O., Dubar, P. D. I., Ramakrishna, M., Scott, K., & Blanchard, H. (2010). Crystallization and preliminary X-ray crystallographic analysis of zebrafish prototype galectin Drgal1-L2. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(12), 1647-1651. doi:10.1107/S1744309110042272

Scopus Eid


  • 2-s2.0-78650125364

Start Page


  • 1647

End Page


  • 1651

Volume


  • 66

Issue


  • 12