Table 1.
Data collection and refinement statistics
| Native | SAD | |
|---|---|---|
| Data collection statistics | ||
| Beamline | BL14.1 - BESSY | ID29 - ESRF |
| Wavelength (Å) | 0.91814 | 1.70 |
| Space group | P 32 2 1 | |
| Cell dimensions a, b, c (Å) | 57.5, 57.5, 118.7 | 57.9, 57.9, 119.7 |
| Resolution (Å) | 49.80–1.59 (1.68–1.59) | 46.24–2.10 (2.21–2.1) |
| Rsym* (%) | 5.1 (44.9) | 6.7 (40.9) |
| I/σI† | 20.6 (4.4) | 24.2 (2.9) |
| Completeness (%) | 98.4 (94.1) | 97.7 (85.9) |
| Redundancy | 9.2 (8.2) | 15.4 (5.6) |
| Phasing statistics (2.5 Å resolution cut-off) | ||
| Anomalous completeness (%) | – | 96.9 (81.2) |
| Anomalous multiplicity | – | 8.3 (3.0) |
| Figure of Merit (FOM) | – | 0.372 |
| Map Skew | – | 0.14 |
| Correlation of local R.m.s. density | – | 0.82 |
| Correlation Coefficient (CC) | – | 0.76 |
| Refinement statistics | ||
| Resolution (Å) | 49.8–1.6 | 31.0–2.10 |
| No. of reflections (work/free) | 29,078/1546 | 13,072/689 |
| Rwork/Rfree‡ (%) | 20.3 (24.0)/22.5 (27.1) | 21.0 (23.3)/26.6 (34.2) |
| No. of atoms/average B-factor | ||
| Protein | 1392/17.6 | 1387/34.33 |
| Water | 119/37.5 | 53/44.61 |
| Other | 99/24.3 | 115/39.90 |
| R.m.s. deviations bond lengths (Å) | 0.016 | 0.018 |
| R.m.s. deviations bond angles (°) | 1.81 | 1.94 |
| Ramachandran plot (% preferred region/% allowed region) | 96.74/3.26 | 95.72/4.28 |
The values in the parentheses refer to the highest resolution shell.
*
Rsym = (∑│Ihkl−<Ihkl>│)/(∑ Ihkl), where the average intensity <Ihkl> is taken over all symmetry equivalent measurements and Ihkl is the measured intensity for any given reflection.
†
I/σI is the mean reflection intensity divided by the estimated error.
‡
Rwork = ││Fo│−│Fc││/│Fo│, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively. Rfree is equivalent to Rwork but calculated for 5% of the reflections chosen at random and omitted from the refinement process.