TABLE 1.
Crystallographic data and refinement statistics for WT ADPRC/ribo-2′F-ADPR
Values in parentheses are from the highest resolution shell.
| Data collection | |
| Cell dimensions a, b, c (Å), α,β,γ (°) | 56.7, 56.7, 360, 90, 90, 120 |
| Space group | P61 |
| Resolution (Å) | 50.0-3.0 (3.11-3.0) |
| Unique reflections | 12475 |
| Multiplicity | 6.6 (6.7) |
| I/σ | 11.84 (2.7) |
| Rmergea (%) | 13.3 (48.8) |
| Completeness (%) | 95.3 (100.0) |
| Refinement | |
| Resolution (Å) | 50.0-3.0 |
| R-factor (%) | 22.1 |
| Rfreeb factor (%) | 26.8 |
| Protein atoms | 4024 |
| Ligands | 2 |
| Mean B-factor for protein atoms (Å2) | 45.5 |
| B-factor for ligands (Å2) | 76 (folded conformation); 70 (extended conformation) |
| r.m.s.c deviations | |
| Bond lengths (Å) | 0.02 |
| Bond angles (°) | 1.99 |
aRmerge = Σ|I − 〈I〉|/ΣI, where I is the integrated intensity of a given reflection.
b Rfree = Σ
Fobs| − |Fcalc/Σ| Fobs|. Rfree was calculated using 5% of data excluded from refinement.
c r.m.s., root mean square.