Table 1.
Crystallographic data collection, phasing and refinement statistics for the isolated A. thaliana HAESA ectodomain.
| HAESA NaI shortsoak | HAESA apo | |
|---|---|---|
| PDB-ID | 5IXO | |
| Data collection | ||
| Space group | P31 21 | P31 21 |
| Cell dimensions | ||
| a, b, c (Å) | 148.55, 148.55, 58.30 | 149.87, 149.87, 58.48 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 |
| Resolution (Å) | 48.63–2.39 (2.45–2.39) | 45.75–1.74 (1.85–1.74) |
| Rmeas# | 0.096 (0.866) | 0.038 (1.02) |
| CC(1/2)# | 100/86.6 | 100/75.6 |
| I/σ I# | 27.9 (4.9) | 18.7 (1.8) |
| Completeness (%)# | 99.9 (98.6) | 99.6 (97.4) |
| Redundancy# | 53.1 (29.9) | 14.4 (14.0) |
| Wilson B-factor (Å2)# | 84.45 | 81.10 |
| Refinement | ||
| Resolution (Å) | 45.75 – 1.74 | |
| No. reflections | 71,213 | |
| Rwork/Rfree$ | 0.188/0.218 | |
| No. atoms | ||
| Protein/glycan | 4,533/126 | |
| Water | 71 | |
| Res. B-factors (Å2)$ | ||
| Protein | 77.54 | |
| Glycan | 95.98 | |
| Water | 73.20 | |
| R.m.s deviations$ | ||
| Bond lengths (Å) | 0.0095 | |
| Bond angles (°) | 1.51 |
Highest resolution shell is shown in parenthesis.
#As defined in XDS (Kabsch, 1993).
$As defined in Refmac5 (Murshudov et al., 1997).