TABLE 1.
Data collection and refinement statistics.
| Parameters | High resolution | Se-peak |
| Synchrotron | 11C Micro-MX, PAL | 11C Micro-MX, PAL |
| Wavelength (Å) | 0.97942 | 0.97942 |
| Space group | C2 | C2 |
| Cell parameters | a = 160.1, b = 100.3, c = 79.6 α = 90.0, β = 113.3, γ = 90.0 | a = 163.7, b = 101.0, c = 82.4 α = 90.0, β = 114.5, γ = 90.0 |
| Resolution (Å) | 20.0 − 1.65 (1.68 − 1.65) | 19.80 − 2.50 (2.54 − 2.50) |
| Completeness (%) | 95.2 (94.1) | 98.2 (99.3) |
| Rmergea (%) | 6.7 (81.4) | 7.6 (16.5) |
| Reflections, Total/Unique | 848,481/131,592 (6498) | 190,169/41,273 (2,073) |
| Multiplicity | 6.5 (5.7) | 4.6 (4.8) |
| Temperature (K) | 100 | 100 |
| I/Sigmab (I) | 17.6 (1.4) | 18.8 (6.3) |
| FOMc, Resolve (20–2.5 Å) | 0.39 | |
| Rfactord/Rfreee | 0.16/0.19 | |
| No. of atoms, protein/water | 1,145/808 | |
| Clashscoref, all atoms | 2.01 | |
| Ramachandran plot | ||
| Favored region (%) | 98.1 | |
| Allowed region (%) | 1.9 | |
| Outliers (%) | 0 | |
| Poor rotamers (%) | 0 | |
| Average B factors (Å2) | ||
| Protein | 22.7 | |
| Solvent | 35.6 | |
| rmsds | ||
| Bonds (Å) | 0.007 | |
| Angles (o) | 1.24 |
Values in parentheses are for the highest-resolution shell. FOM, figure of merit; rmsds, root-mean-square-deviations from ideal values (Engh and Huber, 1991). aRmerge = åhkl[åi (| Ihkl,i-<Ihkl>|)]/åhkl,i<Ihkl>, where Ihkl,i is the intensity of an individual measurement of the reflection with Miller indices hkl and <Ihkl> is the mean intensity of that reflection. bI/Sigma means <I>/σ. cFigure of merit = ∣ P(α)eiα/P(α)∣, where P(α) is the phase probability distribution and α is the phase (100.0-2.75 Å). dRfactor = Σhkl∣∣Fobs∣-∣Fcalc∣∣/Σhkl∣Fobs∣; where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively, for the reflections hkl included in the refinement. eRfree is the same as Rfactor but calculated over a randomly selected fraction (10%) of the reflection data not included in the refinement. f Clashscore is the number of serious steric overlaps (>0.4 Å) per 1,000 atoms. The 100th percentile is the best among the structures of comparable resolution, whereas the 0th percentile is the worst.