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 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.
Murphy
F V
FV
Department of Pharmacology, The University of Colorado Health Sciences Center, 4200 E. Ninth Avenue, Denver, CO 80262 USA.
Sehy
J V
JV
Dow
L K
LK
Gao
Y G
YG
Churchill
M E
ME
D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000737:chemistry* / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D019476:Insect Proteins; D004247:DNA