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Overproduction, crystallization and preliminary crystallographic analysis of a novel human DNA-repair enzyme that recognizes oxidative DNA damage
- 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.
- Subjects :
- DNA Repair
DNA repair
DNA damage
Radical
NEIL1
Biology
Crystallography, X-Ray
DNA Glycosylases
Oxidative dna damage
law.invention
Deoxyribonuclease (Pyrimidine Dimer)
Structural Biology
law
Escherichia coli
Humans
Crystallization
Overproduction
DNA
General Medicine
Molecular biology
Protein Structure, Tertiary
Oxygen
Biochemistry
DNA glycosylase
Electrophoresis, Polyacrylamide Gel
Gene Deletion
DNA Damage
Subjects
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