X-ray crystallography enables detailed structural studies of proteins to understand and
modulate their function. Conducting crystallographic experiments at cryogenic temperatures …

Biomolecules exhibit dynamic behavior that single-state models of their structures cannot
fully capture. We review some recent advances for investigating multiple conformations of …

While protein conformational heterogeneity plays an important role in many aspects of
biological function, including ligand binding, its impact has been difficult to quantify …

Converting cryo-electron microscopy (cryo-EM) data into high-quality structural models is a
challenging problem of outstanding importance. Current refinement methods often generate …

We report for the first time the use of experimental electron density (ED) as training data for
the generation of drug-like three-dimensional molecules based on the structure of a target …

With recent developments in X-ray sources, instrumentation and data-analysis tools, time-
resolved crystallographic experiments, which were originally the preserve of a few expert …

Virtual ligand libraries for ligand discovery have recently increased 10,000-fold. Whether this
has improved hit rates and potencies has not been directly tested. Meanwhile, typically only …

Protein conformational dynamics that may inform biology often lie dormant in high-resolution
electron-density maps. While an estimated∼ 18% of side chains in high-resolution models …

In eukaryotic cells, membrane proteins play a crucial role. They fall into three categories:
intrinsic proteins, extrinsic proteins, and proteins that are essential to the human genome …

In their folded state, biomolecules exchange between multiple conformational states that are
crucial for their function. Traditional structural biology methods, such as X-ray …