Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7.

@article{Muto2007ExpressionPC,
  title={Expression, purification, crystallization and preliminary X-ray analysis of the ligand-binding domain of metabotropic glutamate receptor 7.},
  author={Takanori Muto and Daisuke Tsuchiya and Kosuke Morikawa and Hisato Jingami},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2007},
  volume={63 Pt 7},
  pages={627-30}
}
Glutamate is the major excitatory neurotransmitter and its metabotropic glutamate receptor (mGluR) plays an important role in the central nervous system. The ligand-binding domain (LBD) of mGluR subtype 7 (mGluR7) was produced using the baculovirus expression system and purified from the culture medium. The purified protein was characterized by gel-filtration chromatography, SDS-PAGE and a ligand-binding assay. Crystals of mGluR7 LBD were grown at 293 K by the hanging-drop vapour-diffusion… CONTINUE READING