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![[Figure 3]](wa5115fig3mag.jpg)
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Figure 3
(a) The behaviour of the distance score D as a function of the crystal rotation between frames (Δφ). In this experiment several standard 50-frame data collections were carried out from the same crystal of thaumatin using the same data-collection parameters except for the beam transmission, which was changed to imitate different diffraction strengths. D was then calculated between pairs of images and plotted against Δφ. The rotation per frame was 0.02°. The average crystal mosaicity was 0.04° as determined by XDS (Kabsch, 2010  ). Different colours show the results with different X-ray beam transmissions (from 100% in blue to 0.1% in yellow). (b) A histogram of the distance scores obtained between randomly selected distant images from the same rotational data set. Several data sets from thaumatin, thermolysin and lysozyme crystals were used with different crystal mosaicities and their histograms were summed. |
![[Figure 3]](wa5115fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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