Co-crystallization and preliminary crystallographic analysis of the high mobility group domain of HMG-D bound to DNA

Structural studies are essential to understand mechanisms of nonsequence-sp ecific DNA binding used by chromosomal proteins. A non-histone high-mobilit y group (HMG) chromosomal protein from Drosophila melanogaster, HMG-D, bind s duplex DNA in a nonsequence-specific fashion. The DNA-binding domain of H MG-D has been co-crystallized with a duplex DNA fragment in the primitive o rthorhombic space group P2(1)2(1)2(1), With unit-cell dimensions a = 43.74, b = 53.80, c = 86.84 Angstrom. Data have been collected to 2.20 Angstrom a t 99 K, with diffraction observed to at least 2.0 Angstrom. Heavy-atom deri vative crystals have been obtained by co-crystallization with oligonucleoti des halogenated at major-groove positions near the end of the DNA.