Cryo-electron microscopy (cryo-EM) of non-crystalline single particles is a biophysical
technique that can be used to determine the structure of biological macromolecules and …

For many years, structure determination of biological macromolecules by cryo-electron
microscopy (cryo-EM) was limited to large complexes or low-resolution models. With recent …

Modeling flexible macromolecules is one of the foremost challenges in single-particle
cryogenic-electron microscopy (cryo-EM), with the potential to illuminate fundamental …

We present a new approach for macromolecular structure determination from multiple
particles in electron cryo-tomography (cryo-ET) data sets. Whereas existing subtomogram …

Single particle cryo-EM excels in determining static structures of protein molecules, but
existing 3D reconstruction methods have been ineffective in modelling flexible proteins. We …

Macromolecular complexes that exhibit continuous forms of structural flexibility pose a
challenge for many existing tools in cryo-EM single-particle analysis. We describe a new …

Structural flexibility and/or dynamic interactions with other molecules is a critical aspect of
protein function. Cryogenic electron microscopy (cryo-EM) provides direct visualization of …

This chapter describes algorithmic advances in the RELION software, and how these are
used in high-resolution cryo-electron microscopy (cryo-EM) structure determination. Since …

Abstract Knowledge of the three-dimensional structures of proteins and other biological
macromolecules often aids understanding of how they perform complicated tasks in the cell …

RELION, for REgularized LIkelihood OptimizatioN, is an open-source computer program for
the refinement of macromolecular structures by single-particle analysis of electron cryo …