The average size of a protein ranges from 283-438 residues in length with many bearing PTMs. Obtaining enough D-protein for crystallization screening (generally in milligram range) remains labor-intensive and uneconomical, typically requiring multiple chemical steps and protein refolding. Nevertheless, racemic protein crystallography of miniproteins remains an excellent method for deciphering molecular interactions, particularly serendipitous intermolecular interactions that deem difficult to obtain using homochiral protein crystallography, solution state NMR and/or computational structure prediction. Perhaps, a more promising avenue is to conduct quasi-racemic crystallography, where a minimal D-protein is used to facilitate crystallization of a larger L-protein with (pseudo-)repeated domains. ). All structures modelled in CCP4MG with data obtained from the protein data bank.