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![[Figure 2]](qq5002fig2mag.jpg)
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Figure 2
(a)–(e) Global damage-effect metrics measured for seven successive complete data sets collected from a xylose isomerase crystal at 100 K. (a) The unit-cell volume, (b) the relative Wilson B-factor, (c) Rmeas, (d) CC1/2 and (e) the relative diffraction intensity as the summed reflection intensity of a data set divided by that of the first data set, In/I1, all as a function of average diffraction-weighted dose (Zeldin, Brockhauser et al., 2013  ). Reproduced from Taberman et al. (2019). (f) SynchWeb (Fisher et al., 2015) display as shown in ISPyB of the automatic analysis of the number of spots and the resolution as a function of image number (rotation angle), which vary as the crystal volume changes during the rotation for data collection from two different protein crystals: (i) an undamaged data set and (ii) a damaged data set demonstrating the characteristic decrease in number of spots by the end of the sweep. (g) Scaling factor and Rmerge as a function of image number: (i) an undamaged data set, characterized by the metrics returning to their initial level after 360° rotation (image number 3600), and (ii) a damaged data set, in which Rmerge rises steeply by the end of the collection sweep. A low scaling factor indicates weak diffraction. |
![[Figure 2]](qq5002fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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