Because proteins are the most common targets for drug development, detailed understanding of protein structure is essential for rational design of therapeutic treatments. Currently, X-ray crystallography accounts for 89% of structures deposited in the Protein Data Bank and continues to provide significantly higher resolution than other techniques. However, the availability of suitable 3D protein crystals is a fundamental bottleneck. To access the huge numbers of unsolved protein structures, there is an urgent need for new techniques and materials that can generate crystals across a wide range of proteins. Because the formation of suitable protein crystals is critically determined by the initial nucleation, a promising way for evoking protein crystal growth is to use porous materials. Applying a theoretical method which employs equilibration between the cohesive and the destructive energies of a crystal, it is shown that to get 3D crystals it is vital to have 2D crystals nucleating in a pore first. Experimental studies, stimulated from the theoretical considerations, widen the palette of porous materials which can promote protein crystallization.