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Updated: Jan 27, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
Published on: July 6, 2019
Rigid-body motion is the main source of diffuse scattering in protein crystallography
T de Klijn1, A M M Schreurs1, L M J Kroon-Batenburg1
1Crystal and Structural Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Abstract:
The origin of diffuse X-ray scattering from protein crystals has been the subject of debate over the past three decades regarding whether it arises from correlated atomic motions within the molecule or from rigid-body disorder. Here, a supercell approach to modelling diffuse scattering is presented that uses ensembles of molecular models representing rigid-body motions as well as internal motions as obtained from ensemble refinement. This approach allows oversampling of Miller indices and comparison with equally oversampled diffuse data, thus allowing the maximum information to be extracted from experiments. It is found that most of the diffuse scattering comes from correlated motions within the unit cell, with only a minor contribution from longer-range correlated displacements. Rigid-body motions, and in particular rigid-body translations, make by far the most dominant contribution to the diffuse scattering, and internal motions give only a modest addition. This suggests that modelling biologically relevant protein dynamics from diffuse scattering may present an even larger challenge than was thought.
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