Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis
Mh. Godsey et al., Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis, ACT CRYST D, 56, 2000, pp. 1456-1458
The N-terminal DNA-binding domain of the multidrug transporter activation p
rotein (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 Angstrom. Diffraction data have been collected at 100
K to 2.75 Angstrom resolution at a synchrotron-radiation source.