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  • Title: Purification, functional characterization, and crystallization of the ligand binding domain of the retinoid X receptor.
    Author: Bourguet W, Ruff M, Bonnier D, Granger F, Boeglin M, Chambon P, Moras D, Gronemeyer H.
    Journal: Protein Expr Purif; 1995 Oct; 6(5):604-8. PubMed ID: 8535152.
    Abstract:
    The ligand binding domain (LBD) of the human retinoid X receptor alpha (hRXR alpha) was overproduced in Escherichia coli and purified to more than 95% purity and functional homogeneity. Circular dichroism spectra of the purified RXR alpha LBD indicated that the protein was composed predominantly of alpha-helical structures and coils. Crystals were grown from ammonium citrate using the vapor diffusion method against a reservoir containing 100 mM Pipes (pH 7.0) and 1.5 M ammonium citrate. They belong to the hexagonal space group P6(3)22 with unit cell parameters a = b = 110.8 A and c = 109.9 A, alpha = beta = 90 degrees, gamma = 120 degrees, and they diffract X rays to a resolution limit of 2.5 A using synchrotron radiation. The asymmetric unit of the crystals contains one molecule with a solvent content of approximately 55% and a Vm value of 3.6 A3/dalton.
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