Table 1.
Data and refinement statistics
| A. Data collection statistics | CofE | CofE+GDP+Mn |
| Space group | P41212 | P41212 |
| Unit cell dimensions | ||
| a (Å) | 100.39 | 98.37 |
| b (Å) | 100.39 | 98.37 |
| c (Å) | 92.96 | 94.35 |
| Wavelength (Å) | 0.9794 | 0.9794 |
| Resolution (Å) | 40–2.50 | 40–1.35 |
| No. observed reflections | 34,373 | 823,035 |
| No. unique reflections | 16,992 | 190,592 |
| Rmergea (%) | 8.9 (43.6) | 5.5 (48.9) |
| Completeness (%) | 99.9 (99.2) | 98.7 (97.9) |
| I/Σ | 22.8 (4.0) | 22.3 (4.7) |
| B. Phasing | ||
| Phasing method | SAD | MR |
| Resolution range (Å) | 40–3.0 | 40–3.0 |
| No. SeMet residues | 8 | 0 |
| Phasing statistics | Phasing power 1.53 |
R-factor 0.44; CCb 0.48 |
| C. Refinement statistics | ||
| Resolution range (Å) | 40.0–2.50 | 40.0–1.35 |
| Rcryst (%) | 19.4 | 16.0 |
| Rfree (%) | 25.5 | 19.0 |
| No. non-hydrogen atoms | 3704 | 4784 |
| No. protein atoms | 3603 | 4076 |
| GDP ions | – | 2 |
| Mn ions | – | 4 |
| Solvent ions | 98 | 586 |
| RMSD from target values | ||
| Bond lengths (Å) | 0.020 | 0.012 |
| Bond angles (deg) | 1.83 | 1.56 |
| Average B factors Protein main chain (Å2) | 25.2 | 17.6 |
| Protein side-chain (Å2) | 28.3 | 20.5 |
| Mn | – | 12.3 |
| GDP | – | 11.9 |
| H2O | 44.3 | 33.9 |
Numbers in parentheses are values for the highest-resolution bin.
a
Rmerge = ΣhklΣi | Ii–<I>/ΣhklΣi | <I> |, where Ii is the intensity for the ith measurement of an equivalent reflection with indices h, k, and l.
b
CC, correlation coefficient.