Instrument-model refinement in normalized reciprocal-vector space for X-ray Laue diffraction
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Instrument-model refinement in normalized reciprocal-vector space for X-ray Laue diffraction. / Kaminski, Radoslaw; Szarejko, Dariusz; Pedersen, Martin N.; Hatcher, Lauren E.; Laski, Piotr; Raithby, Paul R.; Wulff, Michael; Jarzembska, Katarzyna N.
In: Journal of Applied Crystallography, Vol. 53, 10.2020, p. 1370-1375.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Instrument-model refinement in normalized reciprocal-vector space for X-ray Laue diffraction
AU - Kaminski, Radoslaw
AU - Szarejko, Dariusz
AU - Pedersen, Martin N.
AU - Hatcher, Lauren E.
AU - Laski, Piotr
AU - Raithby, Paul R.
AU - Wulff, Michael
AU - Jarzembska, Katarzyna N.
PY - 2020/10
Y1 - 2020/10
N2 - 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.
AB - 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.
KW - data processing
KW - Laue diffraction
KW - instrument models
KW - refinement
KW - X-ray diffraction
KW - TIME
KW - ALGORITHM
KW - PROTEIN
KW - PUMP
KW - CRYSTALLOGRAPHY
KW - PHOTOCHEMISTRY
KW - REFLECTIONS
KW - COMPLEXES
KW - TOOLKIT
KW - LIGHT
U2 - 10.1107/S1600576720011929
DO - 10.1107/S1600576720011929
M3 - Journal article
C2 - 33122973
VL - 53
SP - 1370
EP - 1375
JO - Journal of Applied Crystallography
JF - Journal of Applied Crystallography
SN - 0021-8898
ER -
ID: 250542268