Structural and biochemical studies explain the topoisomerase V DNA relaxation mechanism by showing that it adopts an unusual conformation when bound to DNA that exposes the active site.

The crystal structure of Pur-alpha in complex with DNA reveals its molecular mechanisms of nucleic-acid binding and unwinding, allowing for a better understanding of its essential role in neurons.

The structure of the recombination complex responsible for flagellar antigen switching in Salmonella enterica, and the mechanism that regulates the site-specific DNA inversion reaction, have been determined.

A structural analysis of the transcription regulator Mot1 in complex with promoter DNA and the proteins TBP and NC2 provides a first structural framework for how a Swi2/Snf2 type remodeler interacts with a histone fold protein:DNA complex.

Experimental mapping of the joint sequence space of an ancient transcription factor (TF) and its DNA binding sites reveals that epistasis across the molecular interface permitted the evolution of a new and specific TF-DNA complex.

X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

CryoEM structures of open gyrase A dimers and DNA in two states representing steps either prior to or after passage through the DNA-gate, show where a putative T-segment is found.

The crystal structure of human Holliday junction resolvase GEN1 in complex with DNA reveals a conserved chromodomain as an additional DNA-anchoring point that opens new perspectives for enzyme regulation.

New cryoEM structures reveal how small bacteriophage proteins suppress bacterial immunity.

Analysis of genome integrity in primary murine B-cells reveals how depleting 26S proteasome activity enhanced cell survival following treatment with topoisomerase poisons.