I will review efforts to model motions of crystalline proteins using diffuse X-ray scattering. This work requires analysis of raw diffraction images, which are mostly inaccessible in public databases. There is an abundance of potential metadata from these studies, including information about the analysis methods, measurements of diffuse intensity, and results from the modeling. The time is now ripe for integrating diffuse scattering into traditional crystallography: modern beam lines and detectors are enabling higher quality data collection; computations which were previously inaccessible are now becoming feasible; and current protein crystal structure determination methods are approaching the limit of what is possible using the Bragg peaks alone. The deposition of raw images and associated metadata in public databases is a key step in enabling analysis of diffuse scattering for all protein crystallography studies.