TY - JOUR
AU - Fukuyama, Keiichi
AB - A DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8 was crystallized by the vapor‐diffusion method using lithium sulfate as the precipitant and β‐octylglucoside as an additive. The crystals belong to the trigonal space group P3121 or P3221, with unit‐cell dimensions of a = b = 136.0 and c = 108.1 Å. The crystal is most likely to contain one UvrB protein in an asymmetric unit with the Vm value of 3.8 Å3 Da−1. The crystals diffracted X‐rays beyond 2.9 Å resolution. Although the crystals were sensitive to X‐ray irradiation at room temperature, the frozen crystals at 100 K showed no apparent decay during the intensity measurement.
TI - Crystallization and preliminary X‐ray diffraction studies of a DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8
JF - Acta Crystallographica Section D
DO - 10.1107/S0907444998015777
DA - 1999-03-01
UR - https://www.deepdyve.com/lp/wiley/crystallization-and-preliminary-x-ray-diffraction-studies-of-a-dna-O2pbmkNfO9
SP - 704
VL - 55
IS - 3
DP - DeepDyve
ER -