A comparison between electron density multipole parameters from several high-resolution X-ray diffraction analyses of peptides is presented. The parameters of the same type of atoms in the same chemical environment are statistically equal. Therefore, these average parameters were used as fixed parameters in a conventional X-ray refinement of two low-order data sets of pGlu-Phe-D-Pro-phi[CN4]-Me (T = 125 K, sin theta/lambda < 0.65 Angstrom(-1); room temperature, sin theta/lambda < 0.76 Angstrom(-1)). After this refinement, the thermal displacement parameters are physically meaningful, and difference Fourier maps reveal the deformation density of the molecule. Further application of this transferability is molecular modeling and calculation of electrostatic potential of big peptides or proteins as soon as an experimental electron density data bank is available.