This folder contains four examples of merging crystallographic intensities with a bivariate prior: time-resolved Laue crystallography of the photoactive yellow protein (pyp.zip) anomalous diffraction from serial XFEL crystallography of thermolysin (thermolysin_xfel.zip) anomalous diffraction from Laue crystallography of NaI-soaked lysozyme (lysozyme.zip) fragment screening monochromatic data of Nsp3 Mac1 (dfs.zip) Additionally, we provide several auxilliary examples: For PYP, an example where we set aside a test fraction to semi-independently optimize the double-Wilson r (pyp_test_fraction.zip) for lysozyme, two examples, one where we use Laue-DIALS instead of precognition (lysozyme-laue-dials.zip), and another where we set aside the first 90 images to semi-independently optimize the double-Wilson r (lysozyme_test_fraction.zip) For thermolysin, an example where we use a bivariate versus a univariate prior as the number of scaled images grows (thermolysin_xfel_frames_sweep.zip), and another where we set aside the first 395 images to semi-independently optimize the double-Wilson r (thermolysin_xfel_test_fraction.zip) Finally, we provide zip files containing Careless repositories (careless_041.zip, careless_053.zip) and the dw repository containing Jupyter notebooks outlining the theory of the double-Wilson model (dw.zip). Every example includes scripts to run Careless as well as to analyze the outputs in order to reproduce the figures in the double-Wilson manuscript. For every example, there is a `README.md` that describes the contents of each example folder.