In most sexually reproducing organisms, crossing over between chromosome homologs during meiosis is essential to produce haploid gametes. Most crossovers that form in meiosis in budding yeast result from the biased resolution of double Holliday junction (dHJ) intermediates. This dHJ resolution step involves the actions of Rad2/XPG family nuclease Exo1 and the Mlh1-Mlh3 mismatch repair endonuclease. I provide genetic evidence in baker’s yeast that Exo1 promotes meiotic crossing over by protecting DNA nicks from ligation. Using an approach involving extensive mutagenesis I demonstrated the requirement of Exo1 DNA binding for the formation of crossovers in meiosis. Mutations that disrupt protein interactions in DNA binding domains and the hydrophobic wedge conferred significant crossover defects. Extensive mutation of the catalytic domain of Exo1 was unable to disrupt wild-type levels of crossing over, providing more conclusive data that the catalytic activity of Exo1 is dispensable for its role in meiosis. Only mutations within the structural elements in Exo1 that interact with DNA, such as those required for the bending of DNA during nick/flap recognition, are critical for its role in crossing over. Consistent with these observations, meiotic expression of the Rad2/XPG family member Rad27 partially rescued the crossover defect in exo1 null mutants, and meiotic overexpression of Cdc9 ligase reduced the crossover levels of exo1 DNA-binding mutants to levels that approached the exo1 null. In addition, tetrad dissection of exo1 mutants identified a role for Exo1 in crossover interference. Together, these data provide experimental evidence for Exo1-protected nicks being critical for the formation of meiotic crossovers and their distribution.