Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage.

Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Research Abstract Details 

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Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Abstract Text:

M Sugahara,T Mikawa,R Kato,K Fukuyama,T Kumasaka,M Yamamoto,Y Inoue,S Kuramitsu,

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.

Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Publishing Authors By Initials

M Sugahara,T Mikawa,R Kato,K Fukuyama,T Kumasaka,M Yamamoto,Y Inoue,S Kuramitsu,

For similar bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus: thermus thermophilus research abstracts see: bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus: thermus thermophilus research

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Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 127

Page Numbers: 9-11

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 2000

Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Keywords Mesh Terms:

KEYWORDS: Thermus thermophilus

MESH TERMS: enzymology

Chemical & Substance for Abstract: Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage. Information

Substance Name: DNA-Formamidopyrimidine Glycosylase

Registry Number: EC 3.2.2.23

Grant and Affiliation Information for Crystallization and preliminary X-ray crystallographic studies of Thermus thermophilus HB8 MutM protein involved in repairs of oxidative DNA damage.

AFFILIATION: Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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