Table 1.
Crystallographic data and refinement statistics of the RBPMS RRM in the free state and bound to RNA
| Protein/RNA | RBPMS (14–111) L81M | RBPMS (14–111)/UCACU |
|---|---|---|
| Data collection | SeMet | Native |
| Space group | C2221 | P21 |
| Cell dimensions | ||
| a, b, c (Å) | 83·5, 90·9, 47·5 | 30·8, 90·23, 34·16 |
| a, b, g (°) | 90, 90, 90 | 90, 93·7, 90 |
| Resolution (Å) | 60–1·79 | 90–1·8 |
| Rmerge | 9·8 (99·1) | 12·0 (77·5) |
| I/σI | 17·0 (2·2) | 10·3 (1·8) |
| Completeness (%) | 99·9 (99·8) | 99·4 (99·8) |
| Redundancy | 8·5 (8·7) | 6·3 (4·3) |
| Total unique | 16298 (943) | 17527(2559) |
| Refinement | ||
| Resolution (Å) | 60–1·79 | 20–1·95 |
| No. reflections (free) | 17 448 (882) | 13 266 (656) |
| Rwork/Rfree | 20·7/23·9 | 19·0/24·0 |
| Residues | ||
| Protein | 182 | 186 |
| RNA | – | 9 |
| H2O/cation | 144/0 | 138/2 |
| B-factors | 28·7 | 28·0 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0·009 | 0·008 |
| Bond angles (°) | 1·3 | 1·2 |