Table 1.
Crystallographic data collection and refinement statistics of UvsX30–358.
| Data Collection | Native | SAD |
|---|---|---|
| Wavelength (Å) | 1.0 | 0.97931 |
| Space group | P61 | P61 |
| Unit Cell (Å) | a=b=95.97 c=131.27 | a=b=95.48 c=132.30 |
| Resolution (Å) | 83.04 - 2.35 | 50 - 2.8 |
| Mosaicity (°) | 0.549 | 1.157 |
| Unique Reflections | 28005 | 16391 |
| Redundancy | 7.9 | 14.4 |
| Completeness (%)* | 99.3 (92.8) | 97.2 (81.2) |
| I/σ*† | 29.5 (3.2) | 27.4 (2.1) |
| Rsym (%)*‡ | 5.9 (34.5) | 11.6 (44.9) |
| Refinement | ||
| Rcrystal / Rfree(%)*§ | 21.0/24.8 (31.1/36.3) | |
| Average B-Factors (Å2) | ||
| Chain A (Protein) | 23.08 | |
| Chain B (Protein) | 23.13 | |
| Chain C (Water) | 28.40 | |
| Chain D (PO4) | 42.43 | |
| Ramachandran (%) | ||
| Favored | 92.2 | |
| Allowed | 7.8 | |
| Outliers | 0 | |
| Rmsd | ||
| Bond Length(Å) | 0.018 | |
| Bond Angles(°) | 1.759 | |
| Chirality | 0.127 |
*
Values in parentheses are from the highest resolution shell.
†
I/σ is the mean reflection intensity divided by the estimated error.
‡
Rsym = (Σ|Ihkl − <I>|)/(ΣIhkl), where the average intensity <I> is taken over all symmetry equivalent measurements and Ihkl is the measured intensity for any given reflection.
§
Rcrystal = ||Fo| − |Fc||/|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
Rfree is equivalent to Rcrystal, but calculated for 5% of the reflections chosen at random and omitted from the refinement process.