The molecular details of the formation of the myelin sheath, a multilayered membrane in the nervous system, are to a large extent unknown. P2 is a peripheral membrane protein from peripheral nervous system myelin, which is believed to play a role in this process. X‐ray crystallographic studies and complementary experiments have provided information on the structure–function relationships in P2. In this study, a fully deuterated sample of human P2 was produced. Crystals that were large enough for neutron diffraction were grown by a ten‐month procedure of feeding, and neutron diffraction data were collected to a resolution of 2.4 Å from a crystal of 0.09 mm3 in volume. The neutron crystal structure will allow the positions of H atoms in P2 and its fatty‐acid ligand to be visualized, as well as shedding light on the fine details of the hydrogen‐bonding networks within the P2 ligand‐binding cavity.