Table 1.
Crystallographic statistics.
| Data collection | APLF/XRCC4 SeMet |
|---|---|
| Space group | P 212121 |
| Cell dimensions | |
| a, b, c (Å) | 38.50 58.54 94.93 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Wavelength (Å) | 0.98050 |
| Resolution (Å) | 30.0–1.38 (1.42–1.38)a |
| Rmergeb | 5.3 (39.9) |
| I/σ I | 26.7 (3.7) |
| Completeness (%) | 97.8 (80.4) |
| Redundancy | 6.5 (5.1) |
| Refinement | |
| Resolution (Å) | 28.0–1.38 |
| No. reflections | 43,936 |
| Rworkc/Rfreed (%) | 13.7/17.4 |
| No. atoms | |
| Protein | 1736 |
| Ligand/ion | 147 |
| Water | 402 |
| B-factors | |
| Protein | 14.5 |
| Ligand/ion | 26.3 |
| Water | 33.4 |
| R.m.s deviations | |
| Bond lengths (Å) | 0.011 |
| Bond angles (°) | 1.36 |
a
Statistics for outer resolution shell.
b
Rmerge = ∑ hkl ∑ i | Ii − I |/∑hkl∑Ii where Ii is the intensity of the ith measurement of a reflection with indexes hkl and I is the statistically weighted average reflection intensity.
c
R-work = ∑||Fo| − |Fc||/∑|Fo| where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
d
Rfree is the R-factor calculated with a random 5% of the reflections omitted from refinement.