TABLE 1.
Data collection and refinement statistics for the crystal structure of varv F
| Data collection | |
| Space group | I4(1)32 |
| Cell dimensions | |
| a, b, c (Å) | 84.08, 84.08, 84.08 |
| α, β, γ (°) | 90, 90, 90 |
| Resolution (Å) | 30-1.80 (1.86-1.80)a |
| No. observations | 178,276 |
| No. unique reflections | 4,978 |
| Rmergeb | 0.061 (0.252) |
| (I)/σ(I) | 15.1 (8.9) |
| Completeness (%) | 99.9 (99.6) |
| Redundancy | 35.8 (35.6) |
| Refinement | |
| Resolution (Å) | 30-1.80 (1.86-1.80) |
| No. reflections | 4,863 |
| Rfactorc | 0.224 (0.243) |
| Rfreed | 0.244 (0.261) |
| No. atoms | |
| Peptide | 202 |
| Water | 45 |
| B-factors | |
| Peptide | 21 |
| Water | 36 |
| Root mean square deviations | |
| Bond lengths (Å) | 0.004 |
| Bond angles (°) | 1.8 |
a
Highest resolution shell is shown in parentheses
b
Rmerge = Σhkl(Σi(|Ihkl,i – 〈Ihkl〉|))/Σhkl,i〈Ihkl〉, where Ihkl,i is the intensity of an individual measurement of the reflection with indices hkl, and 〈Ihkl〉 is the mean intensity of that reflection
c
Rfactor = Σ||Fo| – |Fc||/Σ|Fo|, where |Fo| and |Fc| are the observed and calculated structure factor amplitudes
d
Rfree is calculated as for Rfactor with 5% of the data excluded from refinement