Abstract
A simple yet efficient instrument-model refinement method for X-ray diffraction data is presented and discussed. The method is based on least-squares minimization of differences between respective normalized (i.e. unit length) reciprocal vectors computed for adjacent frames. The approach was primarily designed to work with synchrotron X-ray Laue diffraction data collected for small-molecule single-crystal samples. The method has been shown to work well on both simulated and experimental data. Tests performed on simulated data sets for small-molecule and protein crystals confirmed the validity of the proposed instrument-model refinement approach. Finally, examination of data sets collected at both BioCARS 14-ID-B (Advanced Photon Source) and ID09 (European Synchrotron Radiation Facility) beamlines indicated that the approach is capable of retrieving goniometer parameters (e.g. detector distance or primary X-ray beam centre) reliably, even when their initial estimates are rather inaccurate.
Original language | English |
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Pages (from-to) | 1370-1375 |
Number of pages | 6 |
Journal | Journal of Applied Crystallography |
Volume | 53 |
DOIs | |
Publication status | Published - 1 Oct 2020 |
Keywords
- Data processing
- Instrument models
- Laue diffraction
- Refinement
- X-ray diffraction
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)