Table 2. Data collection and refinement statistics for N-TXNIP structure.
| N-TXNIP | SeMet_N-TXNIP | |||
|---|---|---|---|---|
| Data collection | ||||
| Space group | P212121 | P212121 | ||
| Cell dimensions | ||||
| a, b, c (Å) | 37.43, 56.62, 67.66 | 37.30, 56.86, 67.80 | ||
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 | ||
| Peak | Inflection | Remote | ||
| Wavelength | 1.0000 | 0.9795 | 0.9796 | 0.9840 |
| Resolution (Å) | 50–1.6 (1.66–1.6)* | 50-1.8 (1.86–1.8) | 50–1.8 (1.86–1.8) | 50–1.8 (1.86–1.8) |
| Rsym (%) | 8.3 (41.6) | 11.7 (66.8) | 9.1 (57.9) | 9.2 (77.8) |
| I/σI | 27.12 (2.28) | 15.15 (2.7) | 35.41 (3.69) | 24.36 (1.93) |
| Completeness (%) | 97.0 (90.5) | 99.9 (99.6) | 100 (99.9) | 99.7 (97.5) |
| Redundancy | 6.0 (4.3) | 10.1 (7.2) | 13.6 (11.5) | 10.1 (5.9) |
| Refinement | ||||
| Resolution (Å) | 18.0–1.6 | |||
| No. reflections | 18,976 | 13,873 | 13,947 | 13,975 |
| Rwork/Rfree | 0.171/0.227 | |||
| No. atoms† | ||||
| Protein | 1,203 | |||
| Waters | 100 | |||
| Average B-factors (Å2) | ||||
| Protein | 23.90 | |||
| Water | 39.32 | |||
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.008 | |||
| Bond angles (°) | 1.129 | |||
| Geometry (%) | ||||
| Favoured region | 90.6 | |||
| Allowed region | 9.4 | |||
*Values in parentheses are for the highest-resolution shell.
†Total number of atoms in an asymmetric unit.