Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA‐repair enzyme that recognizes oxidative DNA damage | Zendy

Bandaru Viswanath | Zendy; Cooper Wendy | Zendy; Wallace Susan S. | Zendy; Doublié Sylvie | Zendy

Open Access

Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA‐repair enzyme that recognizes oxidative DNA damage

Author(s) -

Bandaru Viswanath,

Cooper Wendy,

Wallace Susan S.,

Doublié Sylvie

Publication year - 2004

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444904007929

Subject(s) - dna glycosylase , dna damage , base excision repair , dna repair , dna , ap endonuclease , escherichia coli , microbiology and biotechnology , dna (apurinic or apyrimidinic site) lyase , biology , biochemistry , chemistry , gene

DNA glycosylases repair oxidative DNA damage caused by free radicals. Recently, NEIL1, a human homolog of Escherichia coli DNA glycosylase endonuclease VIII, has been identified and shown to exhibit broad substrate specificity for a variety of types of pyrimidine‐base damage. An active C‐terminal deletion construct of NEIL1 was overexpressed in E. coli and crystallized. The unliganded NEIL1 crystallizes in space group R 3, with unit‐cell parameters a = b = 132.2, c = 51.1 Å. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4 Å, respectively.

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