Crystallization and Preliminary X-Ray Analysis of the Human Androgen Receptor Ligand-Binding Domain with a Coactivator-Like Peptide and Selective Androgen Receptor Modulators

The document described the successful cloning, overproduction, and crystallization of the human androgen receptor ligand-binding domain (hAR LBD) with a coactivator-like peptide and two different selective androgen receptor modulators (SARMs). The crystals obtained were isomorphous, in the space group P2₁2₁2₁, and provided high-resolution diffraction to 1.7 and 1.95 Å. The research aimed to shed light on how nonsteroidal androgens bind compared to steroidal ligands and their selectivity for different tissues. The ligand's role was crucial for maintaining protein stability during purification, and the addition of a coactivator-like peptide and lithium sulfate was essential for the crystallization process. Data sets were collected from the crystals, and the structures were being solved using molecular replacement, with the refinement process still underway at the time of writing.