DNA-binding proteins play a crucial role in all living organisms by interacting 
with various DNA sequences across the genome. While several methods have been 
used to study the interaction between DNA and proteins in vitro, chromatin 
immunoprecipitation followed by sequencing (ChIP-seq) has become the standard 
technique for identifying the genome-wide location of DNA-binding proteins in 
vivo. However, the resolution of standard ChIP-seq methodology is limited by the 
DNA fragmentation process and presence of contaminating DNA. A significant 
improvement of the ChIP-seq technique results from the addition of an 
exonuclease treatment during the immunoprecipitation step (ChIP-exo) that lowers 
background noise and more importantly increases the identification of binding 
sites to a level near to single-base resolution by effectively footprinting 
DNA-bound proteins. By doing so, ChIP-exo offers new opportunities for a better 
characterization of the complex and fascinating architecture that resides in 
DNA-proteins interactions and provides new insights for the comprehension of 
important molecular mechanisms.