SAXS4COLL is an interactive computer program for reduction and analysis of small-angle X-ray scattering data from fibrous collagen tissues, combining data reduction, bespoke background subtraction, semi-automated peak detection and calibration.

MuscleX is an integrated, open-source computer software suite for data reduction of X-ray fiber diffraction patterns from striated muscle as well as other fibrous systems.

Full pattern analyses of small-angle X-ray and neutron scattering data with both discrete reflections and central diffuse scattering are presented. Data with both equatorial streaks and two- and four-point reflections can be fitted in elliptical coordinates with relatively few parameters.

A theoretical formulation for the diffraction from nonuniformly strained helical molecular assemblies is presented. The predictions of this theory are discussed in the context of double-stranded DNA and actin filaments in the presence and absence of nonuniform strains.

ForMAX is a new beamline at the MAX IV Laboratory, providing multiscale and multimodal structural characterization by combining small- and wide-angle X-ray scattering with full-field tomographic imaging.

The high scattering power of a sample at low angles may lead to significant secondary scattering contributions in the measured small- and ultra-small-angle X-ray scattering patterns. A correction procedure is presented for the removal of the excess intensity and to improve the dynamic range of the measurement.

Methods are described for processing XFEL data from individual crystalline fibrils. The methods are applied to data collected at the Linac Coherent Light Source from an amyloid-forming oligopeptide from the adenovirus shaft.

Synchrotron nano-diffraction coupled with electron diffraction and spectroscopic techniques revealed the crystal structure of zeolite erionite from Cappadocia. These results fill in the gap for precise modelling of the carcinogenicity of this killer fibre.

An infrared free-electron laser was applied to dissociate amyloid fibrils of a peptide as a goal of the development of a novel therapeutic strategy for amyloidosis. Solid evidence for β-sheet to α-helix conversion in the peptide fibril by vibrational excitation of amide bonds was obtained by both experiment and molecular dynamics simulation.

Coherent X-ray diffraction imaging and 3D X-ray fluorescence were used to visualize in 3D the self-transformation of polycrystalline microspheres of calcium carbonate into hollow and core-shell microspheroid hierarchical structures.