We use numerical linked cluster expansions (NLC) and exact diagonalization to study confinement transitions out of the quantum spin liquid phase in the pyrochlore-lattice Ising antiferromagnet with random transverse fields. We calculate entanglement entropies associated with local regions defined by single tetrahedron to observe these transitions. The randomness-induced confinement transition is marked by a sharp reduction in the local entanglement and a concomitant increase in Ising correlations. In NLC, it is studied through the destruction of loop resonances due to random transverse-fields. The confining phase is characterized by a distribution of local entanglement entropies, which persists to large random fields.

Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4 Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.