Table 1.
Crystallographic data collection and refinement statistics.
| SeMet CEP441–140 (peak) | SeMet CEP1921743–2092 (peak) | |
|---|---|---|
| Data collection | ||
| Space Group | P41212 | P61 |
| Cell dimensions | ||
| a,b,c (Å) | 33.9, 33.9, 243.4 | 104.6, 104.6, 90.2 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 120.0 |
| Wavelength (Å) | 0.97928 | 0.97835 |
| Resolution (Å) | 81.12–2.30 (2.38–2.30) a | 90.58–2.08 (2.14–2.08) a |
| Rmerge | 0.084 (2.354) | 0.101 (1.311) |
| Rpim | 0.019 (0.506) | 0.024 (0.357) |
| I/σI | 17.7 (1.9) | 19.7 (2.5) |
| Completeness (%) | 100.0 (100.0) | 100.0 (100.0) |
| Redundancy | 21.4 (22.0) | 18.6 (14.4) |
| Wilson B-factor (Å2) | 71.6 | 36.8 |
| Refinement | ||
| Resolution (Å) | 33.62–2.30 (2.48–2.30) | 90.58–2.08 (2.14–2.08) |
| No. reflections | 7072 (1190) | 32002 (2368) |
| Rwork / Rfree | 0.2262/0.2645 | 0.2120/0.2236 |
| Number of atoms | 980 | 2735 |
| Protein | 976 | 2563 |
| Ligand / ion | N/A | 12 |
| Waters | 4 | 162 |
| B-factors | 103.1 | 45.9 |
| Protein | 103.2 | 45.8 |
| Ligand / ion | N/A | 55.1 |
| Waters | 77.5 | 46.6 |
| R.m.s. deviations | ||
| Bond length (Å) | 0.004 | 0.002 |
| Bond Angles (°) | 0.558 | 1.171 |
a A single crystal was used for the structure determination. Values in parentheses are for the highest-resolution shell.