Structural basis for proton transport by EhHv1

Voltage-gated proton channels (Hvs) lack a canonical pore, prompting fundamental questions about how they sense voltage and conduct protons. Despite extensive research, no high-resolution Hv structure is available. Here, we aim to determine the structure of EhHv1, an Hv from the marine coccolithophore Emiliania huxleyi, a key player in carbon cycling. We purified full-length EhHv1 in GDN detergent, confirmed its dimeric state via SEC-MALS and crosslinking, and optimized vitrification during the INSTRUCT Cryo-EM Course (ESRF, May 2025). We now seek SOS pipeline access at CM01 to proceed from on-site frozen UltrAuFoil grids to data collection and analysis with CM01 support.