Table 2.
Structure refinement
| Data | ||
| Resolution range, Å | 28.4-1.90 | |
| Reflections | Working set | 160,479 |
| Free set | 3,189 | |
| Completeness, % | 92.3 | |
| σ-cutoff | 0.0 | |
| Atoms in model | ||
| Protein (nonhydrogen) | 3,928 | |
| β-octylglucoside | 40 | |
| Sulfate | 20 | |
| Water | 270 | |
| Refinement parameters | ||
| Rwork*, % | 24.0 | |
| Rfree*, % | 25.9 | |
| Average atomic B factors, Å2 | ||
| Protein | 35.9 | |
| β-octylglucoside | 52.9 | |
| Sulfate | 65.9 | |
| Water | 41.6 | |
| Deviation from ideality, rms deviation | ||
| Bonds, Å | 0.013 | |
| Angles, ° | 1.504 | |
| Dihedrals, ° | 23.047 | |
| Inpropers, ° | 1.019 | |
* R = 100(Σ|Fobs − Fcalc|)/(ΣFobs), where Fobs and Fcalc are observed and calculated structure factors, respectively.