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  • Title: Purification of the human RARgamma ligand-binding domain and crystallization of its complex with all-trans retinoic acid.
    Author: Rochel N, Renaud JP, Ruff M, Vivat V, Granger F, Bonnier D, Lerouge T, Chambon P, Gronemeyer H, Moras D.
    Journal: Biochem Biophys Res Commun; 1997 Jan 13; 230(2):293-6. PubMed ID: 9016769.
    Abstract:
    A 28-kDa fragment (residues 178-423) of the human retinoic acid receptor gamma, hRARgamma D3E, encompassing the ligand-binding domain (LBD) was overproduced in Escherichia coli and purified as a monomer to more than 95% purity and homogeneity. The Kd for all-trans retinoic acid binding was 0.6 +/- 0.1 nM. Crystals of the LBD complexed with all-trans retinoic acid were grown at pH 7 from sodium acetate in the presence of detergents using the vapor diffusion method. They diffract to 2.0 A using a synchrotron radiation (lambda=0.91 A) and belong to the tetragonal space group P4(1)2(1)2 with unit cell parameters a=b=60.6 A and c=155.3 A, one monomer per asymmetric unit, a solvent content of ca. 33%, and a Vm value of approximately 2 A3/dalton.
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