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- Title
Crystallization and Preliminary X-Ray Crystallographic Studies of Thermus thermophilus HB8 MutM Protein Involved in Repairs of Oxidative DNA Damage.
- Authors
Sugahara, Mitsuaki; Mikawa, Tsutomu; Kato, Ryuichi; Fukuyama, Keiichi; Kumasaka, Takashi; Yamamoto, Masaki; Inoue, Yorinao; Kuramitsu, Seiki
- Abstract
MutM protein, which removes the oxidatively damaged DNA base product, 8-oxogua-nine (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 (CEDES) buffer, pH9.8. The diffraction data derived from oscillation photographs indicate that the crystals belong to the monoclinic system and space group P21. The crystals have unit-cell dimensions of α = 45.4 ε, b = 62.0 ε, c = 99.7 ε and β = 90.8+. Assuming that the asymmetric unit contains two molecules, the Vm value was calculated to be 2.35 ε3.Damins1. The crystals diffracted X-rays to at least 2.1 ε resolution and were suitable for high-resolution X-ray crystal structure determination.
- Subjects
CRYSTALLOGRAPHY; NUCLEIC acids; DNA damage; THERMUS thermophilus; BIOCHEMICAL genetics
- Publication
Journal of Biochemistry, 2000, Vol 127, Issue 1, p9
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a022588