Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis.
The N-terminal DNA-binding domain of the multidrug transporter activation protein (MtaN) was crystallized by the hanging-drop vapour-diffusion method using lithium chloride as a precipitant. The crystals are orthorhombic and belong to the space group I2(1)2(1)2(1), with unit-cell parameters a = 49.4, b = 67.8, c = 115. 0 A. Diffraction data have been collected at 100 K to 2.75 A resolution at a synchrotron-radiation source.
Godsey
M H
MH
Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, Oregon, 97201-3098, USA.
Baranova
N N
NN
Neyfakh
A A
AA
Brennan
R G
RG
D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism*; D011487:Protein Conformation
D001426:Bacterial Proteins; D004247:DNA