TABLE 1.
Diffraction, structure determination, and refinement statistics
| Parameter | Data |
|---|---|
| Diffraction data | |
| Space group | P21 |
| Cell dimensions | a = 37.45 Å, b = 55.50 Å, c = 108.93 Å, β = 91.39° |
| Wavelength (Å) | 0.9792 |
| Spacing limit (Å) | 1.8 |
| Unique reflections | 41,654 |
| Rmerge (%)a | 10.8 (38.6) |
| I/σ | 17.7 (7.1) |
| Completeness (%) | 99.9 (99.9) |
| Anomalous completeness (%) | 99.9 (99.9) |
| Multiplicity | 10.4 (8.9) |
| Phasing and refinement | |
| Bragg spacings (Å) | 28-1.8 |
| Figure of merit after | |
| RESOLVE | 0.75 |
| No. of protein atoms | 3,851 |
| No. of solvent atoms | 482 |
| No. of hetero-atoms (ADP-ribose) | 35 |
| Rwork/bRfreec (%) | 15.1/19.5 |
| Avg B factor (Å2) | 10.613 |
| Rms deviation of bond lengths (Å) | 0.018 |
| Rms deviation of bond angles (°) | 1.85 |
| Ramachandran plotd | 91.1/8.9 |
a
Rmerge = Σ|I − <I>|/Σ I, where I is the observed intensity and <I> is the average intensity. Values in parentheses refer to the highest-resolution shell (1.9 to 1.8).
b
R = Σ ∥Fo| − |Fc∥/Σ|Fo|.
c
Rfree is calculated as R, but on 5% of all reflections that are never used in crystallographic refinement.
d
The percentage of residues located in the most favorable/additionally allowed regions of the Ramachandran plot is given.