Table 2.
Crystallographic data collection and refinement statistics.
| Caspase3/Ac-LDESD-CHO | Caspase7/Ac-LDESD-CHO | |
|---|---|---|
| Space group | P212121 | P3221 |
| a (Å) | 67.37 | 88.64 |
| b (Å) | 93.56 | 88.64 |
| c (Å) | 97.62 | 187.71 |
| β (°) | 90 | 120 |
| Resolution range | 50–1.61 | 50–2.45 |
| Total observations | 358,844 | 175,449 |
| Unique reflections | 72,895 | 28,712 |
| Completeness | 90.1 (63.9)a | 90.3 (57.3)a |
| <I/σ(I)> | 15.3 (2.4) | 18.5 (2.7) |
| Rsym (%)b | 7.5 (41.6) | 9.5 (38.9) |
| Resolution range | 10–1.61 | 10–2.45 |
| Rcryst (%)c | 17.4 | 20.1 |
| Rfree (%)d | 22.3 | 24.8 |
| Mean B-factor (Å2) | 32.4 | 64.2 |
| Number of atoms | ||
| Protein | 3803 | 3777 |
| Inhibitor | 84 | 84 |
| Water | 276 | 82 |
| r.m.s. deviations | ||
| Bond length (Å) | 0.009 | 0.006 |
| Angles | 0.029(Å)e | 1.35(°)f |
a
Values in parentheses are given for the highest resolution shell
b
Rsym = Σhkl|Ihkl − 〈Ihkl〉|/ΣhklIhkl.
c
R = Σ|Fobs − Fcal|/ΣFobs.
d
Rfree = Σtest(|Fobs| − |Fcal|)2/Σtest|Fobs|2.
e
The angle rmsd in SHELX97 is indicated by distance in Å.
f
The angle rmsd in CNS is indicated by angle in degree.