Table 1. X-ray data collection and refinement table.
| Data Collection | MBP-NLRP12 PYD |
| Spacegroup | P21212 |
| Unit cell (a, b, c) (Å) | 103.62, 186.74, 52.72 |
| (α, β, γ) (°) | 90, 90, 90 |
| Wavelength (Å) | 0.97 |
| Wilson B-factor (Å2) | 19.4 |
| Anisotropy | 0.242 |
| Resolution (last shell) (Å) | 50–1.70 (1.80–1.70) * |
| No of reflections (total/unique) | 670878/110662 |
| Completeness (%) | 97.5 (85.3) * |
| Average multiplicity | 6.1 (3.1) * |
| I/σ(I) | 22.4 (3.7) * |
| Rmerge (%)¶ | 5.1 (28.7) * |
| Refinement | |
| Resolution (Å) | 50–1.70 |
| No. of protein atoms/ average B-factor (Å2) | 7757/ 25.17 |
| No. of hetero atoms/ B-factor (Å2) | 564/ 34.93 |
| Rmsd bond lengths (Å) | 0.007 |
| Rmsd bond angles (°) | 1.00 |
| Rwork† | 0.160 |
| Rfree‡ | 0.201 |
| Ramachandran plot favored/disallowed (%)** | 98.8 /0 |
| PDB code | 4XHS |
¶ Rmerge = Σh Σi |Ii(h) -<I(h)> | / ΣhΣi Ii(h), where Ii(h) and <I(h)> are the ith and mean measurement of the intensity of reflection h.
† Rwork = Σh||Fobs (h)|-|Fcalc (h)|| / Σh|Fobs (h)|, where Fobs (h) and F calc (h) are the observed and calculated structure factors, respectively. No I/σ cutoff was applied.
‡Rfree is the R value obtained for a test set of reflections consisting of a randomly selected 5% subset of the data set excluded from refinement.
**Values from Molprobity server (http://molprobity.biochem.duke.edu/).