Electron scattering properties of biological macromolecules and their use for cryo-EM map sharpening.

ABSTRACT: Resolution-dependent loss of contrast in cryo-EM maps may obscure features at high resolution that are critical for map interpretation. Post-processing of cryo-EM maps can improve the interpretability by adjusting the resolution-dependence of structure factor amplitudes through map sharpening. Traditionally this has been done by rescaling the relative contribution of low and high-resolution frequencies globally. More recently, the realisation that molecular motion and heterogeneity cause non-uniformity of resolution throughout the map has inspired the development of techniques that optimise sharpening locally. We previously developed LocScale, a method that utilises the radial structure factor from a refined atomic model as a restraint for local map sharpening. While this method has

SUBMITTER: Bharadwaj A 

PROVIDER: S-EPMC9642005 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature