We examine the interactions between actively rotating proteins moving in a membrane. Experimental evidence suggests that such rotor proteins, like the ATP synthases of the inner mitochondrial membrane, can arrange themselves into lattices. We show that crystallization is possible through a combination of hydrodynamic and repulsive interactions between the rotor proteins. In particular, hydrodynamic interactions induce rotational motion of the rotor protein assembly that, in the presence of repulsion, drives the system into a hexagonal lattice. The entire crystal rotates with an angular velocity which increases with motor density and decreases with lattice diameter - larger and sparser arrays rotate at a slower pace. The rotational interactions allow ensembles of proteins to sample configurations and reach an ordered steady state, which are inaccessible to the quenched nonrotational system. Rotational interactions thus act as a sort of temperature that removes disorder, except that actual thermal diffusion leads to expansion and loss of order. In contrast, the rotational interactions are bounded in space. Hence, once an ordered state is reached, it is maintained at all times.
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