Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV

Gonzalez, A.; Krojer, T.; Nan, J.; Bjelčić, M.; Aggarwal, S.; Gorgisyan, I.; Milas, M.; Eguiraun, M.; Casadei, C.; Chenchiliyan, M.; Jurgilaitis, A.; Kroon, D.; Ahn, B.; Ekström, J.C.; Aurelius, O.; Lang, D.; Ursby, T.; Thunnissen, M.M.G.M.

doi:10.1107/S1600577525002255

Figure 3
Screenshot of real-time data processing results at MicroMAX, as viewed from the beamline control computers. (a) Real-time view of diffraction patterns superposed with identified spot positions. The panel on the right shows the entire detector frame with resolution rings marking 4.0, 3.0, 2.5 and 2.0 Å. The rectangle in blue corresponds to the zoomed-in region displayed on the left panel. (b) View of the diffraction quality score calculated in Dozor over the two-dimensional grid for a 2D-raster data collection mode. (c) Pie plot showing the results of the real-time estimate of the indexing rate in CrystFEL. The fraction of frames containing one or more indexable crystals is shown in purple and the fraction with no indexable crystals is shown in blue. (d) Real-time spotfinding results from Dozor. The top three plots show the number of detected peaks, the diffraction quality score and the apparent resolution limit as a function of the frame number for the last 500 frames of the current detector run. The bottom three plots show the same indicators for the whole of the current detector run, sampling 1 of 50 frames.

JOURNAL OF
SYNCHROTRON
RADIATION

ISSN: 1600-5775

Volume 32| Part 3| May 2025|

https://doi.org/10.1107/S1600577525002255

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