TABLE 1.
Crystallographic data, phasing, and refinement statistics
Values in parentheses correspond to highest resolution shell. FOM, figure of merit; r.m.s.d., root mean square deviation.
| Native | Selenium peak | |
|---|---|---|
| Diffraction data | ||
| Wavelength (Å) | 1.0 | 0.9795 |
| Space group | C 2 | C 2 |
| Unit cell a, b, c (Å) | 161.7, 71.0, 112.7 | 161.1, 70.8, 113.1 |
| Unit cell α, β, γ (°) | 90.0, 131.23, 90.0 | 90.0, 131.46, 90.0 |
| Resolution (Å) | 2.0-30.7 (2.0-2.07) | 3.2-43.0 (3.2-3.3) |
| Completeness (%) | 98.1 (87.3) | 94.3 (82.1) |
| Multiplicity | 6.9 (4.4) | 7.4 (5.4) |
| Rmergea (%) | 5.7 (46.2) | 5.0 (18.1) |
| I/σ | 22.5 (2.6) | 28.7 (9.8) |
| Phasing | ||
| Number of selenium sites | 6 | |
| FOM, anomalous only | 0.47 | |
| FOM, density modification | 0.71 | |
| Refinement | ||
| Resolution (Å) | 2.0-30.7 (2.05-2.0) | |
| No. of reflections | 63,704 | |
| Completeness (%) | 97.9 (84.0) | |
| No. of residues/waters | 970/396 | |
| Rfactorb (%) | 17.8 (27.7) | |
| Rfreec (%) | 22.0 (34.4) | |
| r.m.s.d. bonds (Å) | 0.007 | |
| r.m.s.d. angles (°) | 1.0 | |
| B-factor protein (Å2) | 43.9 | |
| B-factor solvent (Å2) | 44.6 | |
| Protein Data Bank code | 3P53 | |
a Rmerge = Σhkl(I − I)/ΣI where I and I are the observed and mean intensities, respectively, of all observations of reflection hkl, including its symmetry-related equivalents.
b Rfactor = Σhkl‖Fobs| − |Fcalc‖/Σ|Fobs| where Fobs and Fcalc are the observed and calculated structure factors, respectively, of reflection hkl.
c Rfree, Rfactor calculated for a randomly selected subset of the reflections (5%) that were omitted during refinement.