The last decade has witnessed the explosion of research on redox-controlled cellular and biochemical processes. Whereas the vast majority of these studies have centered on clinical, genetic, and biochemical aspects of redox signaling and regulation inside and outside the cell, a significant number of nuclear magnetic resonance (NMR) and crystallographic studies have been undertaken to obtain an atomic-level understanding of the mechanisms of the redox regulation. This review highlights the recent progress of three-dimensional structure determination of key proteins and protein complexes involved in redox regulation. An increased list of such class of protein structures and their complexes with ligands will provide invaluable insight into the molecular basis of redox-regulatory processes and may be useful for the future development of therapeutic agents for redox-related diseases.