Table 2. X-ray structure data processing and refinement statistics.
| Spacegroup | Monoclinic, P21 |
| x-ray source | MX2, Australian Synchrotron |
| Detector | ADSC Quantum 315 |
| Wavelength (Å) | 13000 eV (0.96Å) |
| Unit-cell parameters (Å, °) | a = 36.8, b = 76.6, c = 51.5 90, α = γ = 90.0, β = 100.2, |
| Diffraction data | |
| Resolution range (Å) | 50.70-1.65 (1.74-1.65) |
| No. of unique reflections | 33864 (4934) |
| No. of observed reflections | 242194 |
| Matthews coefficient, V M (Å3 Da−1) | 2.04 |
| Solvent content (%) | 39.6 |
| Completeness (%) | 100 (100) |
| Data redundancy | 7.2 (7.2) |
| Mean I/σ(I) | 18.3 (4.7) |
| Rmerge (%)* | 10.22(0.447) |
| Rp.i.m. (%)# | 4.1 (17.8) |
| Refinement (42.3–1.65 Å) | |
| R free (%) | 22.5 |
| R cryst (%) | 17.9 |
| Size of R free set (%) | 5 |
| Protein native residues (dimer) | 316 |
| 8-MERCAPTOGUANINE Molecules | 2 |
| Water molecules | 254 |
| RMSD from ideal values: | |
| Bond lengths (Å) | 0.024 |
| Bond angles (°) | 2.16 |
| Mean B factors (Å2) | 14.7 |
| Ramachandran plot | |
| Residues in most favored regions (%) | 91.6 |
| Residues in additionally allowed regions (%) | 8.1 |
| Residues in generously allowed regions (%) | 0.4 |
| Residues in disallowed regions (%) | 0.0 |
*Rmerge = ΣhΣi |Ii(h)−<I(h)>|/ΣhΣiIi (h),
#
Rpim = Σh [1/(N-1)]1/2 Σi |Ii(h)−<I(h)>|/ΣhΣiIi (h).
Values in parentheses refer to the outer resolution shell (1.74-1.65Å).
Where I is the observed intensity, <I> is the average intensity of multiple observations from symmetry-related reflections, and N is redundancy.
Rvalue = _jjFoj _ jFcjj/_jFoj, where Fo and Fc are the observed and calculated structure factors. For Rfree the sum is done on the test set reflections (5% of total reflections), for Rwork on the remaining reflections.