Likelihood-based cryo-EM docking using the emplace_local software is faster and more sensitive than the related em_placement software when the approximate location of a component is known. It is conveniently available through a plugin to the ChimeraX visualization software.

An electron-microscopy model of the SET3 histone deacetylase complex reveals a three-lobe architecture.

ISOLDE is an interactive molecular-dynamics environment for rebuilding models against experimental cryo-EM or crystallographic maps. Analysis of its results reinforces the need for great care when validating models built into low-resolution data.

A standalone system, called PDB-Dev, has been developed for archiving integrative structures and making them publicly available. The paper describes the data standards, the software tools and the various components of the PDB-Dev data-collection, processing and archiving infrastructure.

By employing time-dependent density functional theory for solid-state chemistry, the research presented by Andrii Shyichuk [Acta Cryst. (2023), B67, 437–449] significantly contributes to the understanding of electron/hole traps in doped materials.

RSF1 changes the chromatin-remodeling mode of SNF2h. The RSF complex does not have a nucleosome-recentering capacity and a `critical distance' exists during the action of RSF in vitro; this distance is about 24 base pairs. The RSF complex loosens parts of the nucleosome DNA and undergoes conformational change on linker DNA stimulation.

AutoEMage is a new open-source software package that automates data transfer, preprocessing, real-time display and data monitoring during cryo-electron microscopy (cryo-EM) data collection. It is equipped with an easy-to-use graphical user interface that provides seamless data screening and real-time feedback on data quality and microscope status.

A detailed analysis of rhenium(I) organometallic covalent binding to a model protein is conducted at seven time points over 38 weeks. Changes in the protein structure induced at the Re binding sites over the time series as well as the relationship between the proximity of the solvent channels to the residues containing the highest-occupied Re are described.

Preferred orientation of macromolecules is one of the major issues that are commonly encountered in obtaining isotropic cryo-EM maps. Here, a comprehensive examination was performed of how macromolecule orientations respond to changes in physical factors, such as freezing temperature, and chemical factors, such as the addition of surfactants, for a standard set of macromolecules, which provides insights into their behaviour on grids and can be utilized to address the preferred orientation problem in a systemic manner for any given macromolecule.

The use of AlphaFold2 predictions for the detection and correction of sequence-register errors among protein structures determined using cryo-EM deposited in the Protein Data Bank is described.