Table 2. Crystallization summary table.
Refinement of data done in two steps | Data processed in XDS, scaled in Aimless and used for initial refinement | Data included in the final refinement after anisotropic removal of weak data (STARANISO) |
---|---|---|
Resolution (Å) | 49.3 – 3.00 (3.18 –3.00) | 61.7 – 2.57 (2.94 – 2.57) |
Wavelength (Å) | 0.97625 | 0.97625 |
Space group | P31 2 1 | P31 2 1 |
Unit cell (Å) | a=b=113.8,c=79.1 | a=b=113.75, c=79.2 |
Completeness (%) | 99.6 (99.8) | 55.5 (8.4) |
Redundancy | 3.6 (3.8) | 3.6 (3.2) |
No. of observations / unique reflections | 43 475 / 12 088 | 38 750 / 10 669 |
<I/σ(I)> | 11.6 (1.0) | 13.3 (1.9) |
CC(1/2) (%) | 99.8 (68.8) | 99.9 (69.2) |
Rmerge (I) (%) | 4.6 (132.0) | 4.3 (68.5) |
Rcryst (F) (%) | 19.9 (27.4) | |
Rfree (F) (%) | 26.6 (53.2) | |
No. of non-hydrogen atoms | 2704 | |
No. of water molecules | 10 | |
r.m.s. deviations from ideal geometry: Bond lengths (Å) | 0.015 | |
Bond angles (deg) | 1.9 | |
Mean B-factor protein chain, A, B (Å2) | 74.0, 110.9 | |
Mean B-factor peptide C, D (Å2) | 44.0, 78.1 | |
Mean B-factor (water, Å2) | 71.7 | |
Ramachandran plot quality# | ||
Favored regions (%) | 95.7 | |
Allowed regions (%) | 4.3 | |
Outliers (%) | 0 |
Calculated using a local Molprobity server (Chen et al., 2010).