TACAN (Tension-Activated-ChANnel) has recently been identified as one of the principle pain-sensing channels via mechanotransduction which is referred to the conversion of physical forces into electrical and biochemical signals. TACAN does not share significant sequence similarity to any known class of ion channel and thus represents a novel class of mechanosensitive channels. Presently, the three-dimensional structure of TACAN and its gating mechanism are unknown. Based on bioinformatics sequence analysis, TACAN is expected to comprise 5 or 6 transmembrane helices, a 138 residue N-terminal domain and a 14 residue C-terminal domain that includes a cluster of 9 basic residues. We have been successful in purifying TACAN using three different phospholipid membrane mimetic system; such as detergent (DDM) and peptidisc and Saposin lipid nanoparticles (Salipro). TACAN purified in all three systems was used for cryo-EM. TACAN-Salipro has been the most promising for high resolution data collection. TACAN-Salipro incorporation was optimised and high resolution cryo-EM data was collected on purified fractions. Image processing and 3D reconstruction are in progress. This study will help obtain knowledge about the structure and architecture of the transmembrane domain, the importance of the N-terminal and C-terminal domains in channel function and the essential residues lining the pore-forming helices. The structure of TACAN is essential to understanding the underlying mechanisms of function of this channel which will increase our knowledge of channel structure and open the path to developing potential inhibitors and drugs for chronic pain.