Table 1.
Crystal, Data Collection, and Phasing Statistics
| Apo peak | Apo inflection | Apo remote | Ara-5-P complex | |
|---|---|---|---|---|
| λ (Å) | 0.9795 | 0.9798 | 0.9465 | 0.934 |
| Resolution (Å) | 1.5 | 1.5 | 1.5 | 1.25 |
| Reflections (measured) | 226,333 | 230,065 | 323,503 | 392,371 |
| Reflections (unique) | 60,465 | 60,750 | 62,538 | 90,067 |
| Completeness (%, outer shell) | 93.8 | 94.3 | 97.1 | 40.1 |
| Rmergea (overall) | 0.093 | 0.090 | 0.078 | 0.086 |
| Average I/σ(I)b | 19.4 | 17.26 | 18.9 | 12.40 |
| Phasing powerb | 2.24 | 2.86 | 1.74 | - |
| FOMMADc | 0.4198 | 0.4593 | 0.3323 | - |
| FOMMAD (overall) | 0.7224 | - | ||
| FOM (sf)d | 0.8997 | - |
Both the apo and arabinose-5-phosphate complex forms represent the Se-Met enzyme, and crystallized in space group P1. The unit cell dimensions were a = 42.119 Å, b = 42.120 Å, c = 59.429 Å, α = 89.943°, β = 100.95°, γ = 98.729° for the apo form, and a = 42.049 A, b = 42.400 Å, c = 60.195 Å, α = 90.23°, β = 100.98°, γ = 98.98° for the inhibitor complex.
Rmerge = ΣΣ| Ii − Im |/ΣΣ Ii, where Ii is the intensity of the measured reflection and Im is the mean intensity of all symmetry-related reflections.
Phasing power = FH/ERMS. FP, FPH, and FH are the protein, derivative, and heavy atom structure factors, respectively, and ERMS is the residual lack of closure.
Figure of merit from MAD phasing.
Figure of merit after solvent flipping.