Table 1.
Crystallographic analysis
| Data collection | ||
| Protein | SIRT1•CTR•ADPR•Substrate | SIRT1•CTR apo |
| PDB code | 4KXQ | 4IF6 |
| Synchrotron | SSRL | SSRL |
| Beamline | BL12-2 | BL12-2 |
| Space group | P3221 | P43212 |
| Cell parameters | ||
| a, b, c (Å) | 92.7, 92.7, 97.7 | 115.8, 115.8, 350.5 |
| α, β, γ (°) | 90.0, 90.0, 120.0 | 90.0, 90.0, 90.0 |
| Zn peak | Zn peak | |
| Wavelength (Å) | 1.28210 | 1.2676 |
| Resolution (Å) | 50.0 – 1.85 | 50.0 – 2.65 |
| Rsym (%)b | 4.3 (62.6) | 8.8 (94.3) |
| <I>/<σI>b | 34.3 (2.4) | 18.3 (1.8) |
| Completeness (%)b | 100.0 (99.9) | 97.1 (92.8) |
| No. observations | 406,347 | 541,806 |
| No. unique reflections | 80,328 (8,010) | 68,583 (6,409) |
| Redundancy | 5.1 (4.7) | 7.9 (7.8) |
| Refinement | ||
| Resolution (Å) | 50.0 – 1.85 | 50.0 – 2.65 |
| No. reflections total | 80,282 | 67,954 |
| No. reflections test set | 3,824 (4.76%) | 1982 (2.92%) |
| Rwork/Rfree (%) | 16.8/18.9 | 23.0/26.5 |
| No. atoms | 2,842 | 9,424 |
| Protein | 2,484 | 9,374 |
| Ligand | 47 | 4 |
| Water | 311 | 46 |
| B-factors | ||
| Protein | 39.4 | 30.3 |
| Ligand | 33.8 | 60.6 |
| Water | 45.1 | 8.2 |
| R.m.s. deviations | ||
| Bond lengths (Å) | 0.009 | 0.002 |
| Bond angles (°) | 1.2 | 0.630 |
| Ramachandran plotc | ||
| Favored (%) | 97.7 | 96.1 |
| Additionally allowed (%) | 2.3 | 3.9 |
| Outliers (%) | 0.0 | 0.0 |
| MolProbity score | 1.11 | 2.04 |
a
SSRL, Stanford Synchrotron Radiation Lightsource
b
Highest resolution shell is shown in parentheses
c
As determined by MolProbity60