Table 1.
X-ray data collection and refinement statistics (molecular replacement).
| SRD5A2 with NADP–DHFa | |
|---|---|
| Data collection | |
| Space group | P622 |
| Cell dimensions | |
| a, b, c (Å) | 107.4, 107.4, 103.4 |
| α, β, γ (°) | 90, 90, 120 |
| Resolution (Å) | 50–2.8 (2.85–2.8)b |
| Rmerge | 0.248 (1.274) |
| I/σI | 13.0 (1.05) |
| Completeness (%) | 99.7 (100.0) |
| Redundancy | 9.6 (6.8) |
| Refinement | |
| Resolution (Å) | 50–2.8 (3.19–2.8) |
| No. reflections | 9155 (2857) |
| Rwork/Rfree | 0.239 (0.297)/0.265 (0.336) |
| No. atoms | 2036 |
| Protein | 1926 |
| Ligand/ion | 110 |
| Water | 0 |
| B-factors | |
| Protein | 76.4 |
| Ligand/ion | 66.5 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.003 |
| Bond angles (°) | 0.77 |
aDiffraction data of five crystals were merged.
bValues in parentheses are for highest-resolution shell.