Denoising of high-resolution single-particle electron-microscopy density maps by their approximation using three-dimensional Gaussian functions

J Struct Biol. 2016 Jun;194(3):423-33. doi: 10.1016/j.jsb.2016.04.007. Epub 2016 Apr 13.

Abstract

Cryo-electron microscopy (cryo-EM) of frozen-hydrated preparations of isolated macromolecular complexes is the method of choice to obtain the structure of complexes that cannot be easily studied by other experimental methods due to their flexibility or large size. An increasing number of macromolecular structures are currently being obtained at subnanometer resolution but the interpretation of structural details in such EM-derived maps is often difficult because of noise at these high-frequency signal components that reduces their contrast. In this paper, we show that the method for EM density-map approximation using Gaussian functions can be used for denoising of single-particle EM maps of high (typically subnanometer) resolution. We show its denoising performance using simulated and experimental EM density maps of several complexes.

Keywords: Denoising; Electron microscopy density map; Gaussian functions; Macromolecular complexes; Single particle analysis; Structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cryoelectron Microscopy / methods
  • Cryoelectron Microscopy / standards*
  • Macromolecular Substances / chemistry*
  • Molecular Structure
  • Normal Distribution
  • Protein Conformation
  • Ribosome Subunits, Large / chemistry
  • Signal-To-Noise Ratio*
  • beta-Galactosidase / chemistry

Substances

  • Macromolecular Substances
  • beta-Galactosidase