The crystal structures of amino acids, which are composed of molecules in their zwitterionic tautomers, are usually interpreted in terms of strong NH center dot center dot center dot O hydrogen bond formation between the ammonium and carboxylate groups supported by weaker dispersion or CH center dot center dot center dot O interactions. This view of the factors which promote thermodynamic stability in the crystalline amino acids has been re-examined in two phases of glycine, the trigonal gamma-form, which is the thermodynamically most stable form under ambient conditions, and the epsilon-form, which is generated from gamma-glycine at high pressure. A combination of Hirshfeld surface analysis, periodic DFT, PIXEL and symmetry-adapted perturbation theory calculations indicates that the conventional interpretation of intermolecular interactions in crystalline amino acids phases fails to recognise the over-whelming significance of Coulombic attraction and repulsion. There are no intermolecular interactions in either phase that can plausibly be described as dispersion-based. The interaction energies of molecules connected by so-called CH center dot center dot center dot O H-bonds are far in excess of accepted values for such interactions. Of the 14 closest intermolecular contacts in both phases, six have destabilizing interaction energies: in gamma-glycine a hydrogen bond with 'text-book' NH center dot center dot center dot O contact geometry is part of a destabilising molecule-molecule interaction. The relative stabilities of the phases are best understood not in terms of a series of stabilising atom-atom contacts, but rather as a balance between efficient filling of space in the high-pressure epsilon-phase, and more weakly repulsive electrostatic whole-molecule interactions in the gamma-phase.