The term B-factor, sometimes called the Debye–Waller factor, temperature factor, or atomic
displacement parameter, is used in protein crystallography to describe the attenuation of X …

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

Recent advances in the field of electron cryomicroscopy (cryo-EM) have resulted in a rapidly
increasing number of atomic models of biomacromolecules that have been solved using this …

Advances in high-resolution cryo-electron microscopy (cryo-EM) require the development of
validation metrics to independently assess map quality and model geometry. We report …

Modern protein crystal structures are based nearly exclusively on X-ray data collected at
cryogenic temperatures (generally 100 K). The cooling process is thought to introduce little …

In macromolecular crystallography, the rigorous detection of changed states (for example,
ligand binding) is difficult unless signal is strong. Ambiguous ('weak'or 'noisy') density is …

A long-standing challenge is to understand at the atomic level how protein dynamics
contribute to enzyme catalysis. X-ray crystallography can provide snapshots of …

What conformations do protein molecules populate in solution? Crystallography provides a
high-resolution description of protein structure in the crystal environment, while NMR …

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

Single-structure models derived from X-ray data do not adequately account for the inherent,
functionally important dynamics of protein molecules. We generated ensembles of structures …