The paper:
P. Ahnesorg et al., "XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining," Cell, 124:301-13, 2006. (Cited in 76 papers)
The finding:
When Stephen Jackson at Cambridge University read a 2003 PNAS paper describing a patient's defective DNA repair that didn't involve any known repair proteins, he wondered what was going on. "So we said, let's go fishing," says Jackson. They pulled out a new protein, similar in sequence to the DNA repair protein XRCC4. Jackson's team found that the gene's mutation in a cell line derived from the patient was contributing to the cells' radiosensitivity, often linked to problematic DNA repair.
The structure: Jackson, a member of The Scientist's editorial board, named the protein XRCC4-like factor (XLF). Last year he and his colleagues published the crystal structure of XLF, which "shows it is indeed XRCC4-like in its structure." (EMBO J, e-pub ahead of ...
