TABLE II.
Refinement Statistics for YfiH Structure
| Resolution range (Å) | 55.05–2.01 |
|---|---|
| No. of unique reflections | 27,582 |
| Sigma cutoff | 0.0 |
| R-valuea | 0.179 |
| R-freeb | 0.252 (3071)c |
| RMS deviations from ideal geometry | |
| Bond length (1–2) (Å) | 0.015 |
| Angle (°) | 1.517 |
| No. of atoms | |
| Protein | 4,148 |
| Acetate | 20 |
| Glycerol | 12 |
| Zn | 8 |
| Water | 420 |
| Mean B-factor (Å2) | |
| all atoms | 22.5 |
| Protein atoms | |
| Protein main-chain | 20.5 |
| Protein side-chain | 21.8 |
| Acetate | 21.6 |
| Glycerol | 19.4 |
| Zn | 29.0 |
| Water | 33.2 |
| Ramachandran plot statistics (%) | |
| Residues in allowed regions | 99.0 (479) |
| Residues in disallowed region | 1.0 (4) |
a
R-value = ||Fo| − |Fc||/||Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
b
R-free is equivalent to R value but is calculated for 10% of the reflections (number in the parentheses).
c
Chosen at random and omitted from the refinement process.