Table 1. Data collection and structure refinement statistics.
| Synchrotron/beamline | ESRF ID29 |
| Crystal parameters | |
| Space group | P21212 |
| Cell dimensions (Å) | a = 112.93, b = 49.66, c = 58.48 |
| Angles (û) | α = β = γ = 90° |
| Data collection | |
| Wavelength (Å) | 1.0332 |
| Resolution limit (Å) | 100.0–2.40 (2.53–2.40) |
| Mosaicity | 0.29û |
| Rmerge | 0.15 (0.69) |
| Total number of observations | 140,319 (20,111) |
| Total number unique | 13,409 (1898) |
| Mean I/σI | 15.8 (3.5) |
| Completeness (%) | 99.9 (99.8) |
| Multiplicity | 10.4 (10.6) |
| Refinement | |
| Protein atoms in model | 2173 |
| Solvent atoms in model | 250 |
| Rworking | 0.179 |
| Rfree | 0.228a |
| RMSD from ideal geometry b | |
| Bond lengths (Å) | 0.08 |
| Bond angles (°) | 0.772 |
| Wilson B-factor (Å2) | 38.1 |
| Mean B-factor of protein atoms (Å2) | 29.6 |
| Ramachandran plot | |
| Most favoured (%) | 94.7 |
| Outlier (%) | 0.0 |
| PDB ID code | 2YGT |
Rmerge = Σ|Ii – bIiN|/ΣIi.
Rworking = Σ|Fo – Fc|/ΣFo.
Rfree is the R-factor calculated for the cross-validated test set of reflections.
a
Rfree is 4.9% of reflections.
b
As defined by MOLPROBITY.