A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.

Correlation-driven molecular dynamics provides a fully automated and human-bias-free framework for quantitative interpretation of modern cryo-electron microscopy data.

Extensive benchmarking reveals that errors made when manually building models into near-atomic-resolution cryoEM density may automatically be corrected using an improved Rosetta-based structure refinement method.

New hybrid structure determination methods leveraging the inherent biophysical properties of a macromolecule through molecular dynamics simulations provide accurate and cost-efficient ways of achieving atomic structures from high resolution cryo-electron density maps.

High-resolution maps and models of the bacterial ribosome provide new chemical insights into protein synthesis, and should enable the development of robust tools for cryo-EM structure modeling and refinement.

Using GPUs for the costly computations in cryo-EM enables structure determination in mere days on a single workstation.

Structural and functional analysis reveals the mechanistic basis for mammalian target of rapamycin (mTOR)-dependent roles of DEP domain-containing mTOR interacting protein (DEPTOR) in cancer and metabolic regulation.

The structure of the yeast HOPS tethering complex suggests how this large complex may catalyze fusion by tethering Rab-decorated membranes and promoting the assembly of SNAREs.

Local sharpening of cryo-electron microscopy maps using atomic models can increase the interpretability of densities in cases of resolution variation and facilitates model building and refinement.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.