Table 1. Crystallographic data collection and refinement statistics.
| Data collection | |
| Beamline | SSRF BL17U |
| Wavelength | 0.9796 Å |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 81.49, 64.46, 186.05 |
| α, β, γ (°) | 90, 100.43, 90 |
| Resolution (Å) | 50-3.20 (3.27-3.20) |
| Rmerge (%) | 17.0 (87.6) |
| I / σI | 8.5 (3.0) |
| Completeness (%) | 95.1 (96.7) |
| Redundancy | 5.0 (5.1) |
| Refinement | |
| Resolution (Å) | 37.0-3.20 (3.27-3.20) |
| No. Reflections | 31129 (2576) |
| Rwork / Rfree (%) | 19.2/24.0 |
| No. atoms | |
| Protein | 9798 |
| Glycan | 56 |
| B-factors (Å2) | |
| Protein | 73.1 |
| Glycan | 79.0 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.011 |
| Bond angles (°) | 1.508 |
| Ramachandran plot (%) | |
| Most favored | 84.1 |
| Additionally allowed | 14.8 |
| Generously allowed | 0.9 |
| Disallowed | 0.2 |
Rwork and Rfree are defined by R = Σhkl||Fobs| − |Fcalc||/Σhkl|Fobs|, where h, k, and l are the indices of the reflections (used in refinement for Rwork; 5%, not used in refinement for Rfree) and Fobs and Fcalc are the structure factors, deduced from intensities and calculated from the model, respectively.