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Crystallization and preliminary crystallographic analysis of recombinant human galectin-1

Journal Article


Abstract


  • Galectin-1 is considered to be a regulator protein as it is ubiquitously expressed throughout the adult body and is responsible for a broad range of cellular regulatory functions. Interest in galectin-1 from a drug-design perspective is founded on evidence of its overexpression by many cancers and its immunomodulatory properties. The development of galectin-1-specific inhibitors is a rational approach to the fight against cancer because although galectin-1 induces a plethora of effects, null mice appear normal. X-ray crystallographic structure determination will aid the structure-based design of galectin-1 inhibitors. Here, the crystallization and preliminary diffraction analysis of human galectin-1 crystals generated under six different conditions is reported. X-ray diffraction data enabled the assignment of unit-cell parameters for crystals grown under two conditions, one belongs to a tetragonal crystal system and the other was determined as monoclinic P21, representing two new crystal forms of human galectin-1. © International Union of Crystallography 2007.

Publication Date


  • 2007

Citation


  • Scott, S. A., Scott, K., & Blanchard, H. (2007). Crystallization and preliminary crystallographic analysis of recombinant human galectin-1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(11), 967-971. doi:10.1107/S1744309107050142

Scopus Eid


  • 2-s2.0-36248949021

Start Page


  • 967

End Page


  • 971

Volume


  • 63

Issue


  • 11

Abstract


  • Galectin-1 is considered to be a regulator protein as it is ubiquitously expressed throughout the adult body and is responsible for a broad range of cellular regulatory functions. Interest in galectin-1 from a drug-design perspective is founded on evidence of its overexpression by many cancers and its immunomodulatory properties. The development of galectin-1-specific inhibitors is a rational approach to the fight against cancer because although galectin-1 induces a plethora of effects, null mice appear normal. X-ray crystallographic structure determination will aid the structure-based design of galectin-1 inhibitors. Here, the crystallization and preliminary diffraction analysis of human galectin-1 crystals generated under six different conditions is reported. X-ray diffraction data enabled the assignment of unit-cell parameters for crystals grown under two conditions, one belongs to a tetragonal crystal system and the other was determined as monoclinic P21, representing two new crystal forms of human galectin-1. © International Union of Crystallography 2007.

Publication Date


  • 2007

Citation


  • Scott, S. A., Scott, K., & Blanchard, H. (2007). Crystallization and preliminary crystallographic analysis of recombinant human galectin-1. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(11), 967-971. doi:10.1107/S1744309107050142

Scopus Eid


  • 2-s2.0-36248949021

Start Page


  • 967

End Page


  • 971

Volume


  • 63

Issue


  • 11