Significance The influenza M2 channel is among the smallest proton-selective channels found in nature. High-resolution structures of this channel further our understanding of how protons are transported across a membrane bilayer through a constricted membrane protein environment. This study also has broader implications for the structural interpretation of water in channels using X-ray crystallographic techniques. Previous crystallographic structure determined using synchrotron radiation with cryocooling were biased by the low temperature, and room temperature data collection was limited by radiation damage. These problems have been avoided through room temperature diffraction at an X-ray free-electron laser (XFEL) source.
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Thomaston et al. (2017) studied this question.
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