Extended Data Fig. 3: Cryo-EM density of bison NHA2 ΔN in detergent before and after focused refinement.
From: Structure, mechanism and lipid-mediated remodeling of the mammalian Na+/H+ exchanger NHA2
a. Cryo-EM density map of NHA2ΔN after focused refinement with the 6-TM core transport domain (colored in pink), the dimer domain (colored in green) and the N-terminal domain-swapped helix TM –1 from the neighboring protomer (blue and circled). b. Cryo-EM density map for protomer A before (left) and after (right) focused refinement. The protomer is made up from TM 1 to 13 of one monomer and TM -1 of the other monomer; as such oligomerization contacts are retained in the focused refined map. In TM6 the aspartate residues D277 and D278 (encircled) in TM6 were modeled based on the rotomer position in NapA at pH 8.0 (PDB id: 4BWZ).
