Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage.
MutM protein, which removes the oxidatively damaged DNA base product, 8-oxoguanine (GO), has been crystallized by means of a hanging-drop vapor-diffusion procedure using polyethyleneglycol monomethylether 2000 as a precipitant in 2-(cyclohexylamino) ethanesulfonic acid (CHES) buffer, pH 9.8. The diffraction data derived from oscillation photographs indicate that the crystals belong to the monoclinic system and space group P2(1). The crystals have unit-cell dimensions of a = 45.4 A, b = 62.0 A, c = 99.7 A, and beta = 90.8 degrees. Assuming that the asymmetric unit contains two molecules, the Vm value was calculated to be 2.35 A(3).Da(-1). The crystals diffracted X-rays to at least 2.1 A resolution and were suitable for high-resolution X-ray crystal structure determination.
Sugahara
M
M
Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
Mikawa
T
T
Kato
R
R
Fukuyama
K
K
Kumasaka
T
T
Yamamoto
M
M
Inoue
Y
Y
Kuramitsu
S
S
D003460:Crystallization; D018360:Crystallography, X-Ray; D004249:DNA Damage; D004260:DNA Repair; D043382:DNA-Formamidopyrimidine Glycosylase; D009699:N-Glycosyl Hydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D018384:Oxidative Stress; D016963:Thermus thermophilus / Q000201:enzymology*
D009699:N-Glycosyl Hydrolases; D043382:DNA-Formamidopyrimidine Glycosylase