Murphy, F.V., Sehy, J.V., Dow, L.K., Gao, Y.G., Churchill, M.E. (1999). Co-crystallization and preliminary crystallographic analysis of the high mobility group domain of HMG-D bound to DNA.  Acta Crystallogr. D Biol. Crystallogr. 55(9): 1594--1597.

FBrf0111565

Research paper

Structural studies are essential to understand mechanisms of non-sequence-specific DNA binding used by chromosomal proteins. A non-histone high-mobility group (HMG) chromosomal protein from Drosophila melanogaster, HMG-D, binds duplex DNA in a non-sequence-specific fashion. The DNA-binding domain of HMG-D has been co-crystallized with a duplex DNA fragment in the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell dimensions a = 43.74, b = 53.80, c = 86.84 A. Data have been collected to 2.20 A at 99 K, with diffraction observed to at least 2.0 A. Heavy-atom derivative crystals have been obtained by co-crystallization with oligonucleotides halogenated at major-groove positions near the end of the DNA.