Table 1.
Data collection, phasing, and refinement statistics
| Parametera | Valueb for CgCdc13OB4 |
|---|---|
| Data collection (Se peak) | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 61.815, 38.745, 62.709 |
| a, b, g (°) | 90, 109.021, 90 |
| Wavelength (Å) | 0.97949 |
| Resolution (Å) | 100–2.0 |
| Rmerge | 0.064 (0.162) |
| I/σ | 53.7 (11.9) |
| Completeness (%) | 98.7 (92.3) |
| Redundancy | 7.2 (6.2) |
| Phasing | |
| Figure of merit (anomalous) | 0.26324 (acentric reflections); 0.10262 (centric reflections) |
| Phasing power (anomalous) | 1.781 |
| Refinement | |
| Resolution (Å) | 30–1.90 |
| No. of reflections | 22461 |
| Rwork/Rfree (%) | 0.2059/0.2382 |
| No. of atoms | |
| Protein | 2157 |
| Water | 132 |
| B-factors (Å2) | |
| Protein | 42.655 |
| Water | 46.244 |
| RMS deviations | |
| Bond lengths (Å) | 0.007 |
| Bond angles (°) | 1.075 |
Rmerge = Σ|I − <I>|/ΣI, where I is the observed intensity and <I> is the average intensity of multiple observations of symmetry-related reflections, where RMS is root mean square, phasing power = RMS (|FH|/E), |FH| is the heavy-atom structure factor amplitude, and E is the residual lack of closure error, figure of merit = <ΣP(α)eiα/ΣP(α)>, where α is the phase and P(α) is the phase probability distribution. R = Σ||Fo| − |Fc||/Σ|Fo|, where Fo and Fc are observed and calculated structure factor amplitudes, respectively. Rfree is calculated for a randomly chosen 5% of reflections; Rwork is calculated for the remaining 95% of reflections used for structure refinement.
Values in parentheses are for the highest-resolution shell.