Table 2.
Data collection, phasing, and refinement statistics
| Native | SeMet | |
|---|---|---|
| Data collection | ||
| Space group | P212121 | P212121 |
| Unit cell: a, b, c (Å) | 51.2, 90.7, 246.4 | 51.2, 90.9, 246.2 |
| Resolution (Å)* | 50.00–2.2 (2.24–2.2) | 50.00–2.8 (2.85– 2.8) |
| Total reflections | 359,303 | 169,660 |
| Unique reflections | 58,180 | 25,354 |
| Rsym (%) | 6.3 (67.0) | 6.1 (53.8) |
| I/σ(I) | 19.1 (1.7) | 16.7 (2.1) |
| Completeness (%) | 97.9 (87.6) | 96.0 (88.4) |
| Redundancy | 6.2 (5.1) | 6.0 (5.9) |
| Refinement | ||
| Resolution (Å) | 25.0–2.2 | |
| No. reflections used | 51,874 | |
| Rwork/Rfree‡ | 23.7/26.8 | |
| Number of atoms | ||
| Protein | 7251 | |
| Solvent | 160 | |
| Metal/Nucleotide | 1/23 | |
| B-factors | ||
| Protein | 52.9 | |
| Solvent | 32.4 | |
| Metal/Nucleotide | 54.1/62.3 | |
| R.m.s deviations | ||
| Bond lengths (Å) | 0.011 | |
| Bond angles (°) | 1.54 | |
*
Highest resolution shell is shown in parenthesis.
‡
R-factor = Σ(|Fobs| − k|Fcalc|)/Σ |Fobs|and R-free is the R value for a test set of reflections consisting of a random 5% of the diffraction data not used in refinement.