Crystallisation and preliminary crystallographic analysis of recombinant human galectin-1

Abstract

Galectin-1 is considered 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 over-expression 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 structure-based design of galectin-1 inhibitors. Herein the crystallization and preliminary diffraction analysis of human galectin-1 crystals, generated under six different conditions, is reported. X-ray diffraction data enabled assignment of unit cell parameters for crystals grown under one condition, belonging to a tetragonal crystal system, and definition of another as monoclinic P21, representing two new crystal forms of human galectin-1.