Table 1.
Structural data collection and refinement statistics
| Data | AtlAc |
|---|---|
| Crystal parameters | |
| Space group | P3121 |
| Cell parameters (Å) | a = b = 62.55, c = 93.22 |
| Data quality | |
| Wavelength (Å) | 0.9762 (PX1) |
| Resolution of data (Å) | 46.8–1.45 |
| Unique reflections | 38,042 |
| Rmerge (outer shell)a | 0.06 (0.93) |
| Mean I/sigma (I) (outer shell) | 9.8 (1.1) |
| Completeness (outer shell) % | 99.9 (99.9) |
| CC1/2 (outer shell) | 0.99 (0.76) |
| Multiplicity (outer shell) | 4.7 (4.2) |
| Mean B-factor (Å2) | 20.3 |
| Refinement | |
| Rcrystb | 0.14 |
| Rfreec | 0.17 |
| rmsd 1–2 bonds (Å) | 0.012 |
| rmsd 1–3 angles (°) | 1.539 |
| Ramachandran plot | |
| Favored | 98% |
| Outliers | 0% |
| Protein Data Bank code | 7QFU |
a
Rmerge = (Shkl Si½Ihkl − [Ihkl]½/Shkl Si [Ihkl]).
b
Rcryst = Shkl| |Fo| − |Fc| |/Shkl|Fo|.
c
Rfree is calculated for randomly selected reflections excluded from refinement.