Table 1.
Crystallographic statistics.
| Data collection statistics | |
| Crystal | Caspase-8 DEDs (F122A /I128A) |
| Space group | C2 |
| Unit cell dimensions (Å) | a = 100.5, b = 51.2, c = 52.1 α = 90.0°, β = 116.3°, γ = 90.0° |
| Resolution (Å) | 50.0-1.7 (1.73-1.70) |
| Completeness (%) | 99.7 (100) |
| Observed reflections | 477,168 |
| Unique reflections | 26,340 |
| I/σ (I) | 32.5 (2.6) |
| Rmerge (%)a | 5.2 (28.7) |
| Redundancy | 3.8 |
| Refinement statistics | |
| Resolution range (Å) | 50-1.7 |
| Rcryst/Rfree (%)b | 22.7/25.4 |
| Proteins/Water | 183/143 |
| Rmsd bond length (Å)/angles (°) | 0.005/1.004 |
| Average B-factor (Å2) Ramachandran plot (%) | 47.9 |
| Most favored region | 93.1 |
| Additional allowed region | 6.9 |
| Generously allowed region | 0.0 |
| Disallowed region | 0.0 |
Values in parentheses are for the highest resolution shell. aRmerge = Σ|Ii Im|/ΣIi, where Ii is the intensity of the measured reflection and Im is the mean value of all symmetry-related reflections. bRcryst = S||Fobs| - |Fcalc||/S|Fobs|, where Fobs and Fcalc denotes the observed and calculated structure factor amplitude. Rfree = ΣT||Fobs| - |Fcalc||/ST|Fobs|, where T is a test data set of about 5% of the total reflections randomly chosen and set aside prior to refinement.