TABLE 1.
Crystallographic statistics
| GmSAT | GmSAT-serine | GmSAT-CoA | |
|---|---|---|---|
| Crystal | |||
| Space group | R3 | R3 | C2 |
| Cell dimensions | a = b = 110.87 Å, c = 144.01 Å | a = b = 111.37 Å, c = 143.46 Å | a = 207.08 Å, b = 99.18 Å, c = 120.26 Å; β = 117.2° |
| Data collection | |||
| Wavelength (Å) | 0.979 | 0.979 | 0.979 |
| Resolution range (Å) (highest shell resolution) | 25.0–1.75 (1.80–1.75) | 32.1–1.80 (1.85–1.80) | 38.0–3.0 (3.05–3.0) |
| Reflections (total/unique) | 202,566 / 65,219 | 231,622 / 59,901 | 156,040/42,487 |
| Completeness (highest shell) | 98.8% (100%) | 97.4% (99.4%) | 99.4% (100%) |
| I/σ (highest shell) | 38.7 (3.0) | 33.7 (2.8) | 11.4 (1.9) |
| Rsyma (highest shell) | 4.8% (47.5%) | 5.3% (48.0%) | 7.5% (56.0%) |
| Model and refinement | |||
| Rcrystb/Rfreec | 18.0% /20.6% | 16.7%/19.6% | 22.2%/26.4% |
| No. of protein atoms | 3,704 | 3,694 | 10,525 |
| No. of water molecules | 411 | 465 | 0 |
| No. of ligand atoms | 5 | 24 | 240 |
| Root mean square deviation, bond lengths (Å) | 0.007 | 0.006 | 0.009 |
| Root mean square deviation, bond angles (degrees) | 1.022 | 0.987 | 1.48 |
| Average B-factor (Å2): protein, water, ligand | 39.3, 52.4, 74.9 | 35.2, 48.2, 73.3 | 67.2, 104.0 |
| Stereochemistry: most favored, allowed, outliers | 98.4, 1.6, 0% | 98.4, 1.6, 0% | 93.1, 6.8, 0.1% |
a Rsym = Σ|Ih − 〈Ih〉|/ΣIh, where 〈Ih〉 is the average intensity over symmetry.
b Rcryst = Σ|Fo − 〈Fc〉|/ΣFo, where summation is over the data used for refinement.
c Rfree is defined the same as Rcryst but was calculated using 5% of data excluded from refinement.