Protein electrostatic potential Fourier maps calculated using the transferable aspherical atom model and the independent atom model across resolutions.

ABSTRACT: Common sense tells us that experimental maps of lower (worse) resolution obtained from cryogenic electron microscopy or three-dimensional electron diffraction convey less information than maps of higher (better) resolution. However, information regarding the presence of charged moieties is more visible at lower resolutions. To investigate this phenomenon from a theoretical perspective, we analyzed the effects of truncation of data from the high-resolution end (from 1 Å to 8 Å) on theoretical Fourier images of the electrostatic potential of protein crystals, using both the popular independent atom model (IAM) of scattering factors and the more accurate transferable aspherical atom model (TAAM) combined with the UBDB/MATTS data bank. We compared our findings with those obtained for theoretic

SUBMITTER: Kulik M 

PROVIDER: S-EPMC12573929 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature