Production and characterization of a retinoic acid receptor RARγ construction encompassing the DNA binding domain and the disordered N-terminal proline rich domain.

•A RARγ construct bearing Proline-rich and DBD domains was expressed and purified.•We improved purification yield using extensive centrifugation to avoid protein aggregation.•NMR measurements showed that RARγ Proline-rich domain is disordered in solution.•NMR resonance assignments of the RARγ fragment are provided.