De-icing: recovery of diffraction intensities in the presence of ice rings.
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.
Department of Biochemistry and Molecular Biology, School of Medicine, Oregon Health and Science University, Portland, OR 97239-3098, USA. chapmami@ohsu.edu
Michael S
MS
Chapman
Thayumanasamy
T
Somasundaram
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D007053:Ice / Q000032:analysis*
D007053:Ice