Table 1. Data Collection, Phasing, and Refinement Statistics for Structures.
| apo-SgcE6 | SgcE6-FAD | SgcC | |
|---|---|---|---|
| Data Collection | |||
| Protein Data Bank entry | 4HX6 | 4R82 | 4OO2 |
| space group | P21 | P21 | P212121 |
| cell dimensions | |||
| a, b, c (Å) | 56.37, 213.31, 56.72 | 42.05, 62.83, 70.09 | 99.16, 173.73, 113.86 |
| α, β, γ (deg) | 90.00, 88.83, 90.00 | 90.00, 92.06, 90.00 | 90.00, 90.00, 90.00 |
| wavelength (Å) | 0.97912 | 0.97935 | 0.91165 |
| resolutiona (Å) | 30.10–1.90 (1.93–1.90) | 34.93–1.66 (1.69–1.66) | 47.67–2.63 (2.72–2.63) |
| Rsymb or Rmergec (%) | 9.5 (45.2) | 9.0 (52.1) | 29.6 (231.4) |
| CC1/2 (%) | 99.2 (84.1) | 99.4 (69.5) | 98.0 (17.3) |
| I/σ | 19.5 (2.4) | 22.6 (2.0) | 5.3 (0.62) |
| completeness (%) | 98.3 (80.9) | 99.5 (97.3) | 96.7 (97.9) |
| redundancy | 3.3 (2.8) | 3.7 (2.9) | 5.2 (4.3) |
| Refinement | |||
| resolution (Å) | 30.10–1.90 | 34.93–1.66 | 47.67–2.63 |
| no. of reflections | 104829 | 43097 | 296449 |
| Rwork/Rfree | 0.169/0.212 | 0.164/0.188 | 0.216/0.246 |
| Ramachandran plot (%)d | |||
| favored | 99 | 98 | 95 |
| outliers | 0 | 2 | 0 |
| no. of atoms | |||
| protein | 10513 | 2515 | 15938 |
| ligand/ion | 50 | 176 | 8 |
| water | 774 | 240 | 217 |
| B-factor (Å2) | |||
| protein | 29.0 | 21.1 | 57.1 |
| ligand/ion | 53.8 | 22.4 | 61.9 |
| water | 37.0 | 30.9 | 47.8 |
| root-mean-square deviation | |||
| bond lengths (Å) | 0.007 | 0.006 | 0.002 |
| bond angles (deg) | 1.083 | 1.158 | 0.67 |
a
Numbers in parentheses are values for the highest-resolution bin.
b
Rmerge = ∑hkl∑i|Ii(hkl) – I̅(hkl)|/∑hkl∑iIi(hkl), where Ii(hkl) is the ith observation of reflection hkl and I̅(hkl) is the weighted average intensity for all observations i of reflection hkl.
c
Rmeas = ∑hkl[N/(N – 1)1/2]∑i|Ii(hkl) – I̅(hkl)|/∑hkl∑iIi(hkl).
d
As defined by MolProbity.