Table S2.
Crystallographic statistics
| Native data | TRAF4/GPIbβ |
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c, Å | 56.7, 88.6, 120.7 |
| α, β, γ, ° | 90.0, 93.6, 90.0 |
| Resolution, Å | 50.0–2.5 |
| Rsym, % | 7.7 (26.9)† |
| Mean I/σ, I | 21.7 (3.4)† |
| Completeness, % | 95.0 (95.9)† |
| Redundancy | 3.1 (3.1)† |
| Refinement | |
| Resolution, Å | 33.0–2.5 |
| Molecules/au* | 6 (proteins) and 3 (peptides) |
| No. reflections | 38,763 |
| Rwork/Rfree, % | 21.1/26.4 |
| No. atoms | |
| Protein | 7,805 |
| Water | 29 |
| Average B-factors, Å2 | |
| Chain A | 49.1 |
| Chain B | 60.4 |
| Chain C | 55.1 |
| Chain D | 52.6 |
| Chain E | 56.1 |
| Chain F | 55.0 |
| Chain G | 58.7 |
| Chain I | 60.7 |
| Chain K | 84.8 |
| Water | 52.7 |
| rmsd | |
| Bond lengths, Å | 0.010 |
| Bond angles, ° | 1.390 |
| Ramachandran plot, % | |
| Most favored regions | 96.1 |
| Additional allowed regions | 3.9 |
*
Asymmetric unit.
†
Statistics for the highest resolution shell are shown in parentheses.