TABLE 2.
Data collection and refinement statisticsb
| Statistic type | Native | Selenomethionine derivative |
||
|---|---|---|---|---|
| Peak | Remote | Inflection | ||
| Data collection | ||||
| Wavelength (Å) | 1.0 | 0.9793 | 0.913 | 0.9797 |
| Space group | P1 | P1 | P1 | P1 |
| Cell dimensions | ||||
| a, b, c | 31.56, 37.53, 63.91 | 31.70, 38.13, 64.08 | 31.73, 38.22, 64.13 | 31.71, 38.17, 64.19 |
| Alpha, beta, gamma | 85.45, 82.26, 81.26 | 85.60, 82.06, 81.54 | 85.64, 82.10, 81.28 | 85.56, 82.06, 81.45 |
| Resolution range (Å) | 37.03–1.7 (1.79–1.7)a | 37.65–1.86 (1.96–1.86) | 37.72–1.73 (1.82–1.73) | 37.68–1.86 (1.96–1.86) |
| No. of total reflections | 113,354 (15,961) | 92,762 (13,115) | 114,487 (16,212) | 93,035 (13,094) |
| No. of unique reflections | 29,564 (4,221) | 23,720 (3,384) | 29,331 (4,195) | 23,733 (3,384) |
| Rsym (%) | 0.074 (0.424) | 0.081 (0.617) | 0.092 (0.858) | 0.070 (0.645) |
| Mean I/sigma(I) | 10.8 (2.8) | 9.4 (1.7) | 7.6 (0.8) | 10.8 (1.6) |
| Multiplicity | 3.8 (3.8) | 3.9 (3.9) | 3.9 (3.9) | 3.9 (3.9) |
| Completeness (%) | 93.7 (91.7) | 95.6 (93.5) | 95.4 (93.3) | 95.3 (93.1) |
| Refinement | ||||
| Resolution (Å) | 31.6/1.7 | |||
| R-factor | 0.19 (0.27) | |||
| R-free | 0.21 (0.32) | |||
| No. of atoms | 2,589 | |||
| Macromolecules | ||||
| Protein | 2,168 | |||
| Ligand/ion | 2 | |||
| Water | 419 | |||
| Protein residues | 262 | |||
| B-factors | 29.7 | |||
| Protein | 28.1 | |||
| Solvent | 37.8 | |||
| RMSD | ||||
| Bond lengths (Å) | 0.006 | |||
| Bond angles (°) | 0.879 | |||
| Ramachandran favored (%) | 98.6 | |||
| Ramachandran outliers (%) | 0.39 | |||
| Clash score | 5.57 | |||
a
Values in parentheses are stated for the highest-resolution bin for each structure.
b
Data collection statistics are shown for the native data set and those used for MAD phasing (peak, inflection, and remote). The final model was refined against the native set.