Crystallization and preliminary X-ray diffraction studies of a DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8

A DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8 was crystallized by the vapor-diffusion method using lithium sulfate as the precipitant and beta-octylglucoside as an additive. The crystals belong to the trigonal space group P3(1)21 or P3(2)21, with unit-cell dimensions of a = b = 136.0 and c = 108.1 Angstrom. The crystal is most likely to contain one UvrB protein in an asymmetric unit with the V-m, value of 3.8 Angstrom(3) Da(-1). The crystals diffracted X-rays beyond 2.9 Angstrom resolution Although the crystals were sensitive to X-ray irradiation at room temperature, the frozen crystals at 100K showed no apparent decay during the intensity measurement.