Extended Data Table 1.
Data collection and refinement statistics
| Separase (51–1630)-securin (258–373) complex crystal form I | Separase (71–1630)-securin (258–373) complex crystal form I | Separase (51–1630)-securin (258–373) complex crystal form II | |
|---|---|---|---|
| Data collection | |||
| Space group | P3221 | P3221 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 126.3, 126.3, 273.9 | 125.9, 125.9, 271.9 | 238.4, 89.5, 119.0 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 105.2, 90 |
| Resolution (Å) | 50–3.0 (3.11–3.0)* | 50–2.6 (2.69–2.6)* | 50–3.7 (3.93–3.7) |
| Rmerge (%) | 14.4 (>100) | 14.5 (>100) | 16.6 (232) |
| CC1/2 | (0.480) | (0.476) | (0.271) |
| I/σI | 15.0 (1.5) | 14.4 (1.2) | 4.43 (0.49) |
| Completeness (%) | 99.8 (99.6) | 100 (99.9) | 96.2 (90.9) |
| Redundancy | 10.4 (7.6) | 10.0 (8.2) | 2.7 (2.5) |
| Refinement | |||
| Resolution (Å) | 50–3.0 (3.11–3.0) | 50–2.6 (2.69–2.6) | |
| No. reflections | 51,130 (4,818) | 77,428 (7,588) | |
| Rwork/Rfree (%) | 19.5 (31.4)/25.2 (36.3) | 22.1 (34.6)/26.4 (37.0) | |
| No. atoms | |||
| Protein | 12,609 | 12,633 | |
| Ligand/ion | 0 | 0 | |
| Water | 0 | 16 | |
| B-factors | |||
| Protein | 97.1 | 72.0 | |
| Ligand/ion | - | - | |
| Water | - | 63.2 | |
| R.m.s deviations | |||
| Bond lengths (Å) | 0.003 | 0.011 | |
| Bond angles (°) | 0.65 | 1.2 | |
Two crystals were used for data collection for crystal form I, and one crystal for crystal form II.
*
Highest resolution shell is shown in parenthesis.