De-icing: recovery of diffraction intensities in the presence of ice rings
- Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380 (United States)
Correction for ice-rings in diffraction images is demonstrated as an alternative to exclusion of affected reflections. Completeness can be increased without significant loss of quality in the integrated data. Macromolecular structures are routinely determined at cryotemperatures using samples flash-cooled in the presence of cryoprotectants. However, sometimes the best diffraction is obtained under conditions where ice formation is not completely ablated, with the result that characteristic ice rings are superimposed on the macromolecular diffraction. In data processing, the reflections that are most affected by the ice rings are usually excluded. Here, an alternative approach of subtracting the ice diffraction is tested. High completeness can be retained with little adverse effect upon the quality of the integrated data. This offers an alternate strategy when high levels of cryoprotectant lead to loss of crystal quality.
- OSTI ID:
- 22351208
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 66, Issue Pt 6; Other Information: PMCID: PMC2879358; PMID: 20516627; PUBLISHER-ID: ea5117; OAI: oai:pubmedcentral.nih.gov:2879358; Copyright (c) International Union of Crystallography 2010; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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