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![[Figure 4]](he5693fig4mag.jpg)
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Figure 4
Improving data completeness by merging data collected from crystals in different orientations on the sample grid. (a) Enlarged atlas view showing crystals I and II positioned perpendicular to each other on adjacent grid squares of the same sample. The EM stage tilt axis is vertical, and red arrows show the direction of consecutive data-acquisition regions. (b, c, d) Effect of data completeness on the quality of calculated maps for the Gab1 fragment. Upper panels: reciprocal-space reflection distribution prepared with 3D Data Viewer in Phenix (Liebschner et al., 2019  ). Missing reflections are shown in white and systematic absences in pink; it is evident from the former that the b* axes of both crystals are in the direction of the electron beam. Lower panels: 2Fo − Fc maps (contoured at 1.5σ, blue mesh) for Gab1 residues 624–631 (yellow sticks) in complex with the N-terminal domain of SHP21–222 (gray surface) using phases from the final structure refined against the corresponding data set. (b) Data collected from crystal I (oriented perpendicular to the rotation axis) with a total completeness of 79% results in density for the peptide but misses a significant wedge of data. (c) Crystal II (oriented parallel to the rotation axis) yielded data with a completeness of 55%, resulting in recognisable yet broken density for the peptide. (d) Merging the data from both crystals I and II significantly reduces the missing wedge, resulting in a better-defined density with improved connectivity. |
![[Figure 4]](he5693fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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