Table 1.
Data collection, phasing and refinement statistics
| Native | SeMet Crystal 1 | SeMet Crystal 2 | |||
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | I4 | I4 | I4 | ||
| Cell dimensions | |||||
| a, b, c (Å) | 97.2, 97.2, 45.5 | 97.9, 97.9, 45.5 | 98.0, 98.0, 45.5 | ||
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 |
| Peak | Inflection | Remote | Peak | ||
|---|---|---|---|---|---|
| Wavelength | 0.9793 | 0.9792 | 0.9794 | 0.9757 | 0.9792 |
| Resolution (Å) | 48.6–1.90 (2.00–1.90) | 69.0–2.70 (2.70–2.85) | 69.0–3.00 (3.16–3.00) | 69.0–3.50 (3.69–3.50) | 69.0–3.00 (3.16–3.00) |
| Rsym or Rmerge | 8.70 (61.5) | 8.10 (28.6) | 9.80 (36.6) | 9.80 (24.2) | 9.10 (40.6) |
| I/σI | 13.0 (3.10) | 13.8 (4.40) | 11.1 (3.50) | 11.4 (5.50) | 12.9 (3.80) |
| Completeness (%) | 99.7 (100.0) | 99.3 (98.9) | 99.1 (99.8) | 98.5 (99.7) | 99.9 (100.0) |
| Redundancy | 7.4 (6.9) | 4.0 (3.8) | 3.7 (3.9) | 3.4 (3.6) | 5.6 (5.7) |
| Refinement | |||||
| Resolution (Å) | 1.90 | ||||
| No. reflections | 15 963 | ||||
| Rwork/Rfree | 18.6/23.6 | ||||
| No. atoms | |||||
| Protein | 1621 | ||||
| Ligand/ion | 23 | ||||
| Water | 107 | ||||
| B-factors (Å2) | |||||
| Protein | 29.3 | ||||
| Ligand/ion | 55.8 | ||||
| Water | 36.2 | ||||
| Rmsd | |||||
| Bond lengths (Å) | 0.006 | ||||
| Bond angles (°) | 0.793 |
Values in parentheses are for highest resolution shell.