Table 1 Crystallographic data
From: Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC
Enzyme | FAD/SAM-ecMnmC | FAD- ypMnmC | FAD/SAM-ypMnmC |
|---|---|---|---|
Data Collection | |||
Space Group | P41212 | P21 | P21 |
Cell Dimension | Â | Â | Â |
a, b, c (Ã…) | 100.06, 100.06, 159.19 | 65.15, 59.57, 99.63 | 66.09, 59.82, 100.80 |
α, β, γ (°) | 90, 90, 90 | 90.00, 99.57, 90.00 | 90.00, 100.18, 90.00 |
Resolution (Å) | 50.0–2.55 (2.64-2.55) | 50.0–2.30 (2.37-2.30) | 50.0–2.70 (2.75-2.70) |
I/σ | 9.9 (2.5) | 14.8 (2.6) | 9.3 (2.1) |
Completeness (%) | 100.0 (100.0) | 99.9 (99.9) | 100.0 (100.0) |
Redundancy | 11.9 (12.1) | 6.1 (5.7) | 5.1 (5.2) |
Rmerge | 0.200 (0.964) | 0.083 (0.622) | 0.143(0.734) |
Refinement | |||
Number of used Reflections | 25,161 | 29,178 | 18,983 |
Protein Nonhydrogen Atoms | 5,212 | 4,943 | 4,916 |
Ligand Atoms | 81 | 54 | 81 |
Water Molecules | 222 | 171 | 91 |
Rwork | 0.185 | 0.173 | 0.180 |
Rfree | 0.247 | 0.231 | 0.259 |
Average B-factor, (Ã…2) | 22.47 | 25.69 | 25.82 |
RMSD from Ideal Geometry | Â | Â | Â |
Bond Length (Ã…) | 0.011 | 0.015 | 0.013 |
Bond Angles (°) | 1.41 | 1.48 | 1.49 |