Neutron diffraction is similar to x-ray diffraction in many ways. The main difference is that neutrons interact with the nuclei of atoms instead of electrons. In biological systems hydrogens are easily visualized with neutron scattering where the corresponding x-ray diffraction experiment would need a very high resolution structure to achieve the same result. Furthermore, isotopes scatter neutrons differently allowing for example exchange rate experiments between hydrogen and deuterium.

Recently the sub-angstrom structure of membrane protein AQY1 was published. Since the crystals obtained were stable and easily grown we are now pursuing a crystallization optimization to adapt the protocol for neutron diffraction. This would tell us more about how the waters in the channel are ordered and therefore give more information on the mechanism of water transport in aquaporins.