BACKGROUND Conformational changes are essential for the correct functioning of
biological macromolecules. Time-resolved x-ray crystallography extends an extremely …

A new scientific frontier opened in 2009 with the start of operations of the world's first x-ray
free-electron laser (FEL), the Linac Coherent Light Source (LCLS), at SLAC National …

Dramatic advances in protein structure prediction have sparked debate as to whether the
problem of predicting structure from sequence is solved or not. Here, I argue that AlphaFold2 …

A survey of protein databases indicates that the majority of enzymes exist in oligomeric
forms, with about half of those found in the UniProt database being homodimeric …

Much of our current understanding of how small-molecule ligands interact with proteins
stems from X-ray crystal structures determined at cryogenic (cryo) temperature. For proteins …

X-ray free-electron lasers provide femtosecond-duration pulses of hard X-rays with a peak
brightness approximately one billion times greater than is available at synchrotron radiation …

Molecular recognition by proteins is fundamental to molecular biology. Dissection of the
thermodynamic energy terms governing protein–ligand interactions has proven difficult, with …

Allostery is an inherent feature of proteins, but it remains challenging to reveal the
mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic …

Recent years have witnessed an explosion of interest in understanding the role of
conformational dynamics both in the evolution of new enzymatic activities from existing …

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