Table 1.
Data collection and refinement statistics
| Native | SeMet-SAD | Orthorhombic | |
|---|---|---|---|
| Data collection | |||
| X-ray source | DIAMOND I03 | DIAMOND I02 | SRS 10.1 |
| Wavelength (Å) | 0.97630 | 0.97920 | 1.11700 |
| Space group | P21 | P21 | P21212 |
| Cell dimensions | |||
| a, b, c (Å) | 52.23, 57.71, 85.12 | 52.45, 57.67, 86.22 | 88.73, 116.2, 55.10 |
| α, β, γ (°) | 90, 106.96, 90 | 90, 107.25, 90 | 90, 90, 90 |
| Resolution (Å) | 49.96–2.00 | 49.86–3.00 | 43.43–2.20 |
| (2.11–2.00) | (3.16–3.00) | (2.32–2.20) | |
| Rmerge | 0.101 (0.562) | 0.052 (0.086) | 0.132 (0.424) |
| No. reflections (total) | 237 955 (34 930) | 178 653 (26 231) | 127 598 (17 522) |
| No. reflections (unique) | 32 765 (4744) | 10 020 (1442) | 28 777 (4050) |
| I/σI | 12.8 (3.5) | 47 (29.4) | 8 (3.1) |
| Completeness (%) | 99.9 (99.9) | 99.8 (100) | 98.1 (98.6) |
| Redundancy | 7.3 (7.4) | 9.1 (9.2) | 4.4 (4.3) |
| Refinement | |||
| Resolution (Å) | 2.0 | 2.2 | |
| No. reflections | 32 807 | 29 576 | |
| Rwork/Rfree | 17.87/23.28 | 21.08/26.99 | |
| No. atoms | |||
| Protein | 3422 | 3409 | |
| Ligand/ion | 0 | 91 | |
| Water | 302 | 249 | |
| B-factors | |||
| Protein | 34.785 | 19.689 | |
| Ligand/ion | 38.934 | ||
| Water | 37.651 | 26.411 | |
| R.m.s.d. | |||
| Bond lengths (Å) | 0.0095 | 0.0118 | |
| Bond angles (°) | 1.2112 | 1.3641 |
Figures in parentheses relate to data collected in the highest resolution shell. Note that for the SeMet SAD data sets Bijvoet pairs were not merged.