In this review, we describe recent research developments into radiation damage effects in
macromolecular X-ray crystallography observed at synchrotrons and X-ray free electron …

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

A comprehensive understanding of protein function demands correlating structure and
dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half …

Radiation damage remains one of the major bottlenecks to accurate structure solution in
protein crystallography. It can induce structural and chemical changes in protein crystals …

Radiation damage limits the accuracy of macromolecular structures in X-ray crystallography.
Cryogenic (cryo-) cooling reduces the global radiation damage rate and, therefore, became …

Luminescence methods for non-contact temperature monitoring have evolved through
improvements of hardware and sensor materials. Future advances in this field rely on the …

We introduce a liquid application method for time-resolved analyses (LAMA), an in situ
mixing approach for serial crystallography. Picoliter-sized droplets are shot onto chip …

X-ray crystallography is the gold standard to resolve conformational ensembles that are
significant for protein function, ligand discovery, and computational methods development …

How changes in enzyme structure and dynamics facilitate passage along the reaction
coordinate is a fundamental unanswered question. Here, we use time-resolved mix-and …

New X‐ray crystallography and cryo‐electron microscopy (cryo‐EM) approaches yield vast
amounts of structural data from dynamic proteins and their complexes. Modeling the full …