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Updated: Aug 22, 2026

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
Published on: May 24, 2017
Crystallization of the xeroderma pigmentosum group F endonuclease from Aeropyrum pernix
John Lally1, Matthew Newman, Judith Murray-Rust
1Structural Biology Laboratory, The London Research Institute, Cancer Research UK, 44 Lincolns Inn Fields, London WC2A 3PX, England.
Abstract:
The xeroderma pigmentosa group F protein (XPF) is a founding member of a family of 3'-flap endonucleases that play an essential role in nucleotide-excision repair, DNA replication and recombination. The XPF gene has been cloned from Aeropyrum pernix, encoding a 254-residue protein (apXPF). Recombinant protein was produced in Escherichia coli and purified by three chromatographic steps. Three different crystal forms of apXPF were grown in trigonal, monoclinic and triclinic systems. The trigonal crystals diffracted to 2.8 A and were grown in the presence of double-stranded DNA. Monoclinic crystals were grown without DNA and diffracted to 3.2 A. Triclinic crystals were grown from a truncated apXPF protein lacking the tandem helix-hairpin-helix motifs and diffracted to 2.1 A.
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