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Diffuse X-ray scattering has been an important tool for understanding the atomic structure of binary systems for more than 50 years. The majority of studies have used laboratory-based sources providing 8 keV photons or synchrotron radiation with similar energies. Diffuse scattering is weak, with the scattering volume determined by the X-ray absorption length. In the case of 8 keV photons, this is not significantly different from the typical extinction length for Bragg scattering. If, however, one goes to energies of the order of 100 keV the scattering volume for the diffuse scattering increases up to three orders of magnitude while the extinction length increases by only one order of magnitude. This leads to a gain of two orders of magnitude in the relative intensity of the diffuse scattering compared with the Bragg peaks. This gain, combined with the possibility of recording the intensity from an entire plane in reciprocal space using a two-dimensional X-ray detector, permits time-resolved diffuse scattering studies in many systems. On the other hand, diffraction features that are usually neglected, such as multiple scattering, come into play. Four types of multiple scattering phenomena are discussed, and the manner in which they appear in high-energy diffraction experiments is considered. [ABSTRACT FROM AUTHOR]

Renewed interest in room-temperature diffraction has been prompted by the desire to observe structural dynamics of proteins as they function. Serial crystallography, an experimental strategy that aggregates small pieces of data from a large uniform pool of crystals, has been demonstrated at synchrotrons and X-ray free-electron lasers. This work utilizes a microfluidic crystallization platform for serial Laue diffraction from macroscopic crystals and proposes that a collection of small slices of Laue data from many individual crystals is a realistic solution to the difficulties in dynamic studies of irreversible biochemical reactions.