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

Authors :
Viswanath Bandaru
Wendy Cooper
Susan S. Wallace
Sylvie DoubliƩ
Source :
Acta Crystallographica Section D Biological Crystallography. 60:1142-1144
Publication Year :
2004
Publisher :
International Union of Crystallography (IUCr), 2004.

Abstract

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 A. Complete data sets were collected from native, selenomethionyl and iodinated NEIL1 to 2.1, 2.3 and 2.4 angstroms, respectively.

Details

ISSN :
09074449
Volume :
60
Database :
OpenAIRE
Journal :
Acta Crystallographica Section D Biological Crystallography
Accession number :
edsair.doi.dedup.....d1e0d521cec3d16c327775984b816d17
Full Text :
https://doi.org/10.1107/s0907444904007929