Table 1. Data collection and refinement statistics.
| CD27L Proteolytic fragment | CTP1L V195P mutant (proteolytic fragment)# | ΔN-CD27LHg derivative | |
| Data collection | |||
| Space group | P212121 | I222 | P21 |
| Cell dimensions | |||
| a, b, c (Å) | 75.3, 82.1, 83.8 | 44.9, 48.8, 77.2 | 63.1, 84.7, 65.3 |
| α, β, γ (°) | 90.0, 90.0, 90.0 | 90.0, 90.0, 90.0 | 90.0, 92.0, 90.0 |
| Wavelength (Å) | 0.970 | 1.223 | 0.998 |
| Resolution (Å) | 20–2.24 (2.37–2.24)* | 20–2.10 (2.17–2.10)* | 20–3.5 (3.66–3.50)* |
| R sym or R merge | 12.8 (59.8)* | 2.5 (4.4)* | 23.8 (55.8)* |
| I/σI | 7.0 (2.0)* | 48.9 (29.0)* | 4.7 (2.6)* |
| Completeness (%) | 97.9 (93.8)* | 92 (55.5)* | 99.9 (99.9)* |
| Redundancy | 2.7 (2.6)* | 5.7 (4.4)* | 4.8 (4.8)* |
| Refinement | |||
| Resolution (Å) | 30–2.24 | 20–2.10 | |
| No. reflections | 24189 | 4489 | |
| R work/R free | 18.9/24.7 | 17.2/26.4 | |
| No. atoms | |||
| Protein | 4052 | 645 | |
| Ligand/ion | n/a | n/a | |
| Water | 398 | 90 | |
| B-factors | |||
| Protein | 45 | 22 | |
| Ligand/ion | n/a | n/a | |
| Water | 57 | 32 | |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.01 | 0.01 | |
| Bond angles (°) | 1.3 | 1.0 |
*Values in parentheses are for highest-resolution shell.
#
The data collection was affected by ice rings and a limited detector geometry.