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Diffraction data to 2.45 Å resolution were collected at ESRF Grenoble, France (beamline ID 29).
Data from a native crystal to 2.2 Å and a crystal from selenium-labeled p115GHR to 2.8 Å resolution were collected at 100 K at the Protein Structure Factory beamline 14.2 of the Freie Universität Berlin [21] at BESSY (Berlin, Germany).
For all spectra 56 scan at 4 cm-1 spectral resolution were collected and digitally averaged.
Sections of 2048 x 2048 pixel resolution were collected using the 8-line average bidirectional scanning mode.
Data collection and structure determination: Complete data sets for the wild-type protein (1.15 Å resolution) and the FDC_Ec E72A variant (1.50 Å resolution) were collected at the beamline BM30A[ 37] and ID29[ 38] at the ESRF Grenoble, France.
X-ray intensity data to 1.50 Å resolution were collected at 100K at Diamond Light Source (UK) on macromolecular crystallography beamline I03, and the data processed (Supplementary Table S4) by the XDS package [ 22].
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Information on 104 conflict cases that have been analyzed using the graph model for conflict resolution is collected and stored.
A dataset of ∼2.42×106 µm3 at 72 nm3 voxel resolution was collected.
A complete, high quality dataset to 2.3 Å resolution was collected.
A dataset of ∼1.2×105 µm3 at 24×24×50 nm voxel resolution was collected (Fig. 5B F and Movies S4, S5 and S6 online).
A dataset of ∼3.33×105 µm3 at 56×56×50 nm3 voxel resolution was collected from a 32 hours post fertilization (hpf) embryo (Movie S2 online).
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