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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    
a, b, c (Å) 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, (Å2) 22.47 25.69 25.82
RMSD from Ideal Geometry    
Bond Length (Å) 0.011 0.015 0.013
Bond Angles (°) 1.41 1.48 1.49
  1. Data collection and refinement statistics for the FAD/SAM-bound ecMnmC, FAD-bound ypMnmC and FAD/SAM-bound ypMnmC. Values for the outer resolution shell of data are given in parentheses.