Protein crystallography for aspiring crystallographers or how to avoid pitfalls and traps in macromolecular structure determination

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Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, background): “Since the first protein structures were determined in the 1950s (Kendrew et al., 1958; Perutz et al., 1960), the method has experienced many methodological and technological developments and is now considered to be quite mature (Wlodawer et al., 2013).”
Cryo-EM: Beyond the Microscope (2017, background): “Structurally homogeneous samples can sometimes be prepared by removal of flexible components or by introducing stabilizing mutations, but these may come at the price of steering the samples away from physiologically relevant conditions [23].”
ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps (2018, background): “For any structure, it is generally advisable that human eyes should assess every residue against the density at least once (Wlodawer et al., 2013); quite apart from the need to reduce errors, this increases the chances of identifying unusual sites of potential biological interest.”
Atomic Resolution Structure of a Protein Prepared by Non-Enzymatic His-Tag Removal. Crystallographic and NMR Study of GmSPI-2 Inhibitor (2014, background): “Despite significant methodological progress [1], structural studies of proteins still require significant amount of pure samples.”