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

Highlights•Laboratory directed evolution and ancestral reconstruction can facilitate study of
protein structural dynamics.•Advances in biophysical and computational techniques facilitate …

The creation of artificial enzymes is a key objective of computational protein design.
Although de novo enzymes have been successfully designed, these exhibit low catalytic …

Decades of structure-function studies have established our current extensive understanding
of enzymes. However, traditional structural models are snapshots of broader conformational …

Engineered metalloenzymes represent promising catalysts for stereoselective C–H
functionalization reactions. Recently, P450 enzymes have been evolved to allow for new-to …

Allosteric enzymes contain a wealth of catalytic diversity that remains distinctly underutilized
for biocatalysis. Tryptophan synthase is a model allosteric system and a valuable enzyme for …

Correlated motions of proteins are critical to function, but these features are difficult to
resolve using traditional structure determination techniques. Time-resolved X-ray methods …

Cancer cells frequently exhibit uncoupling of the glycolytic pathway from the TCA cycle (ie,
the" Warburg effect") and as a result, often become dependent on their ability to increase …

Recent technical advances have dramatically increased the power and scope of structural
biology. New developments in high-resolution cryo-electron microscopy, serial X-ray …

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