TABLE 1.
Statistics of the x-ray diffraction data set and refinement of the dscCfaE G168D structure
| dscCfaE G168D | |
|---|---|
| Data statistics | |
| Wavelength (Å) | 0.97856 |
| Space group | C2 |
| Cell dimensions | |
| a/b/c (Å) | 104.06/126.36/78.70 |
| β | 100.49° |
| Resolution (Å) | 50–2.6 |
| No. of unique reflections | 30,301 |
| Rmergea | 0.095 (0.310)b |
| Completeness (%) | 98.4 (89.1) |
| Redundancy | 3.6 (2.4) |
| 〈I/σ〈I〉〉 | 13.0 (2.2) |
| Refinement statistics | |
| Rwork | 0.184 |
| Rfreec | 0.234 |
| No. of residues | 712 |
| No. of protein atoms | 5536 |
| No. of non-protein atoms | 249 |
| Wilson B factor (Å2) | 38 |
| Mean B factor (Å2) | 40 |
| r.m.s.d. bond length (Å) | 0.017 |
| r.m.s.d. bond angle | 1.712° |
| Ramachandran plot (%)d | |
| Favored | 97.3 |
| Allowed | 2.7 |
| Disallowed | 0 |
a Rmerge is defined as Σ|Ih,i − 〈Ih〉|/ΣIh,i, where Ih,i is the intensity for the ith observation of a reflection with Miller index h, and 〈Ih〉 is the mean intensity for all measured values of Ih.
b Numbers in parentheses are for the outer resolution shell (2.69–2.60 Å).
c 5% of total reflections were set aside randomly for the Rfree calculation.