Crystallization and preliminary crystallographic analysis of recombinant human galectin-1.
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 P2(1), representing two new crystal forms of human galectin-1.
Scott
Stacy A
SA
Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland 4222, Australia.
Scott
Ken
K
Blanchard
Helen
H
D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D037483:Galectin 1 / Q000737:chemistry*; D006801:Humans; D008027:Light; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012542:Scattering, Radiation
D037483:Galectin 1; D011994:Recombinant Proteins