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 …

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

New features in the dose estimation program RADDOSE‐3D are summarised. They include
the facility to enter a diffraction intensity decay model which modifies the “Diffraction …

We have studied the fading of electron diffraction spots from two-dimensional (2D) crystals of
paraffin (C 44 H 90), purple membrane (bacteriorhodopsin) and aquaporin 4 (AQP4) at …

An understanding of radiation damage effects suffered by biological samples during
structural analysis using both X-rays and electrons is pivotal to obtain reliable molecular …

Room-temperature macromolecular crystallography allows protein structures to be
determined under close-to-physiological conditions, permits dynamic freedom in protein …

Serial synchrotron crystallography (SSX) is enabling the efficient use of small crystals for
structure–function studies of biomolecules and for drug discovery. An integrated SSX system …

The aim of structural biology has been always the study of biological macromolecules
structures and their mechanistic behaviour at molecular level. To achieve its goal, multiple …

The recent success of electron cryomicroscopy in biology has drawn the attention of the
materials science community, which is starting to employ similar techniques for imaging a …