Table 1.
Crystallography data collection and refinement statistics
| Data collection | RBBP4–BCL11A(2–16) |
|---|---|
| Space group | P212121 |
| Unit cell a, b, c (Å) | 51.301, 85.264, 87.968 |
| Wavelength (Å) | 0.9786 |
| Resolution (Å)a | 2.40 (2.44–2.40) |
| Rsym (%)b | 11.5 (56.6) |
| 〈I/σI〉c | 10 (3) |
| Completeness (%)d | 99.7 (98.7) |
| Redundancy | 8.2 (8.0) |
| Refinement | |
| Resolution (Å) | 2.40 |
| R-factore | 20.1 |
| Rfreef | 24.4 |
| Protein atoms | 2766 |
| Water molecules | 140 |
| Unique reflections | 14917 |
| r.m.s.d.g | |
| Bonds (Å) | 0.010 |
| Angles (°) | 1.08 |
| MolProbity Scoreh | 1.25 |
| Clash Scoreh | 3.01 |
a Statistics for highest resolution bin of reflections are given in parentheses.
b Rsym = ΣhΣj|Ihi − 〈Ih〉|/ΣhΣjIhi, where Ihi is the intensity of observation j of reflection h and 〈Ih〉 is the mean intensity for multiply recorded reflections.
c Intensity signal-to-noise ratio is shown.
d Completeness of the unique diffraction data is shown.
e R-Factor = Σh ‖Fo|−|Fc‖/Σh|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes for reflection h.
f Rfree is calculated against a 10% random sampling of the reflections that were removed before structure refinement.
g Root mean square deviation of bond lengths and bond angles is shown.
h Data are from Chen et al. (43).