Table 2. Data Collection and Refinement Statistics.
| crystal | ChsE4-ChsE5/FADH2a |
|---|---|
| space group | C 1 2 1 |
| cell dimensions | |
| a, b, c (Å) | 185.7, 108.1, 82.0 |
| α, β, γ (deg) | 90.0, 93.0, 90.0 |
| data collectionb | |
|---|---|
| resolution (Å) | 46.4–2.0 (2.00–1.99) |
| wavelength (Å) | 0.9792 |
| reflections | |
| observed | 739 658 (7336) |
| unique | 109 767 (1104) |
| Rmergec | 0.076 (0.624) |
| Rmeasd | 0.082 (0.700) |
| Ranome | 0.057 (0.588) |
| Rpimf | 0.031 (0.262) |
| CC1/2g | 0.999 (0.939) |
| I/σI | 19.9 (2.9) |
| completeness (%) | 99.9 (99.8) |
| multiplicity | 6.7 (6.6) |
| Wilson B | 28.9 |
| refinementb | |
|---|---|
| resolution (Å) | 46.4–2.0 (2.05–1.99) |
| no. reflections | 104 247 (7657) |
| Rwork/Rfree | 0.1508/0.1862 |
| CC*g | 1.000 (0.984) |
| no. atoms | |
| protein | 11 396 |
| FADH2 | 106 |
| solvent | 899 |
| B factors | |
| protein | 36.6 |
| FADH2 | 32.5 |
| solvent | 42.5 |
| RMS deviations | |
| bond lengths (Å) | 0.017 |
| bond angles (deg) | 0.84 |
| Ramachandran | |
| favored (%) | 98 |
| allowed (%) | 2 |
| outliers (%) | 0 |
| PDB ID | 4X28 |
a
See Figure S5.
b
Values in parentheses are for the highest-resolution shell.
c
The merging R factor describes the deviation of an individual intensity measurement from the mean value of all of its symmetry-equivalent reflections.
d
The redundancy-independent merging R factor, Rrim or Rmeas, indicates the precision of an individual intensity measurement independently of the multiplicity of that measurement.
e
The precision-indicating merging R factor, Rpim, describes the precision of the averaged intensity measurement.
f
The anomalous R factor quantifies the relative differences in Friedel-related reflections.
g
CC1/2 and CC* are statistics for assessing the effective resolution limits and quality of diffraction data in the context of a refined model.31