Mirogabalin is a novel potent and selective gabapentinoid drug, and it has been approved for the treatment of peripheral neuropathic pain. The binding target of this drug is identified as a voltage-gated calcium channel auxiliary subunit α₂δ-1. However, the precise binding mode remains unknown. In the present study, we successfully express and purify recombinant human α₂δ-1 protein towards structural analysis and mutational characterization of mirogabalin binding mode. Full length α₂δ-1 constructs with octa-histidine tag insertion were expressed in Expi293 cells and solubilized by the detergent dodecyl maltopyranoside. Screening of orthologues and tag insertion sites identified human α₂δ-1 with the tag after Arg677 as a construct showing well-behaved profile of size exclusion chromatography. Mirogabalin was able to bind to the purified α₂δ-1 by microscale thermophoresis. Our single particle analysis of amphipol-substituted α₂δ-1 by cryo-electron microscopy revealed the map at medium resolution, which resembles to the published structure of α₂δ-1 as a component of rabbit endogenous calcium channel complex. Therefore, our recombinant expression and purification system is indispensable to unveil the ligand binding structure in human α₂δ-1 and mirogabalin complex, although the structure so far analyzed have to be improved.