Gerrit H. U. Lamm

The paper presents cryo-EM structures of FArhodopsin and proteorhodopsin, showing no retinal binding despite conserved lysine and similar fold to retinal-binding rhodopsins, with mutations identified that prevent retinal binding.

The paper characterizes CryoRhodopsins from cold environments, revealing their dual functionality and structural adaptations to low temperatures.

The paper identifies a new subgroup of light-driven sodium pumps with an additional glutamic acid residue that reduces pH sensitivity for sodium transport.