A method is presented to reconstruct the 2D electron densities of fiber cross-sections from disordered small-angle X-ray scattering measurements, combining fiber diffraction theory with physical constraints, like finite cross-section size and non-negative density, in a numerical optimization framework.

The analytical solution of the tilt-angle determination problem in fiber diffraction is presented.

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.

Non-rotationally averaged 3D structures of fibers can be restored from their rotationally averaged diffraction patterns.

By using wide-angle X-ray scattering, contributions from amorphous and crystalline domains are detected separately in cellulose fibers, which enables an accurate determination of regenerated cellulose-fiber crystallinity.

For application in time-resolved wide-angle X-ray diffraction studies, a method for the automatic mapping of fiber diffraction patterns into reciprocal space has been designed.

A cylindrically symmetric model is proposed for the distribution of atomic coordinate errors in helical structures. Formulas for likelihood functions in fiber difraction are presented.

A check of the flat-field calibration of a CCD detector showed good agreement with the manufacturer's calibration. A position-specific effect was detected that requires an additional correction to scale diffraction data properly. The source of this effect is uncorrectable using the flat-field correction, leading to a modulation of sharp features.

Compact, inexpensive, easily constructed sample holders for fiber diffraction allow humidity control, stretching and exposure to magnetic fields during fiber preparation, and primary containment for toxic and infectious biological materials.

This study presents the crystal structure of a ∼320 Å long protein fiber generated by in-frame extension of its repeated helical coiled-coil core.