Table 1. X-ray data collection and refinement statistics.
| ΔNgB-glyco+1G2 Fab | |
|---|---|
| Data collection | |
| Space group | P213 |
| Cell dimensions | |
| a, b, c (Å) | 176.49, 176.49, 176.49 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Resolution (Å) | 50–3.55 (3.74–3.55)* |
| No. of reflections | 1,56,458 (22,493) |
| No. of unique reflections | 22,423 (3,233) |
| Rmerge | 0.104 (1.061) |
| I/σI | 16.4 (2.1) |
| Completeness (%) | 100 (100) |
| Redundancy | 7.0 (7.0) |
| Refinement | |
| Resolution (Å) | 19.983–3.6 |
| No. reflections | 21,341 |
| Rwork/Rfree | 0.212/0.260 |
| No. atoms | |
| Protein | 6,270 |
| Ligand/ion | 141 |
| Water | — |
| B-factors | |
| Protein | 116 |
| Ligand/ion | 180 |
| Water | — |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.005 |
| Bond angles (°) | 1.147 |
| Ramachandran plot† | |
| Favoured | 85.8% |
| Allowed | 11.5% |
| Outliers | 2.7% |
R.m.s. deviation, root-mean-square deviation.
*Values in parentheses are for highest-resolution shell.
†Measured using Molprobity.