Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 60, Issue -, Pages 1142-1144Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444904007929
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Funding
- NCI NIH HHS [R37CA33657] Funding Source: Medline
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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 R3, with unit-cell parameters a=b=132.2, c=51.1 Angstrom. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4 Angstrom, respectively.
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