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. Author manuscript; available in PMC: 2016 Jul 11.
Published in final edited form as: Nat Struct Mol Biol. 2016 Jan 11;23(2):110–115. doi: 10.1038/nsmb.3148

Data Table 1. Data collection and refinement statistics (molecular replacement).

Unmodified
(4X62)
m6A +1
(4X64)
m6A +2
(4X65)
m6A +3
(4X66)
Data collection
Space group P41212 P41212 P41212 P41212
Cell dimensions
a, b, c (Å) 400.8, 400.8, 175.1 400.5, 400.5, 175.5 401.4, 401.4, 175.9 401.3, 401.3, 175.6
 α, β, γ (°) 90, 90, 90 90, 90, 90 90, 90, 90 90, 90, 90
Resolution (Å) 35.0-3.45 (3.51-3.45) 35.0-3.35 (3.41-3.35) 35.0-3.35 (3.41-3.35) 55.0-3.45 (3.51-3.45)
Rmerge 0.168 (0.984) 0.130 (0.993) 0.141 (0.929) 0.210 (0.961)
I / σI 15.10 (2.76) 12.29 (1.25) 19.08 (2.83) 9.04 (1.77)
Completeness (%) 99.2 (100.0 96.4 (91.4) 100.0 (100.0) 96.6 (98.7)
Redundancy 10.5 (10.7) 5,8 (2.7) 11.9 (9.2) 5.1 (4.9)
Refinement
Resolution (Å) 35.0-3.45 (3.49-3.45) 35.0-3.35 (3.38-3.35) 35.0-3.35 (3.38-3.35) 50.0-3.45 (3.49-3.45)
No. reflections 183968 (5548) 171102 (1033) 204105 (5914) 180755 (5622)
Rwork / Rfree 0.181/0.214 (0.272/0.296) 0.165/0.204 (0.291/0.314) 0.185/0.211) (0.261/0.303) 0.194/0.226 (0.297/0.354)
No. atoms
 Protein 19121 19121 19121 19121
 RNA 32874 32875 32875 32875
Ligand/Ion/Water 782 829 844 826
B factors
 Protein 110.3 94.8 77.9 99.4
 RNA 97.8 80.2 66.1 86.5
Ligand/Ion/Water 103.4 83.6 74.6 87.3
r.m.s. deviations
 Bond lengths (Å) 0.004 0.004 0.005 0.005
 Bond angles (°) 0.790 0.859 0.819 0.801

One crystal was used for each dataset. aValues in parentheses are for highest-resolution shell.

[AU: Equations defining various R values are standard and hence are no longer defined in the footnotes.]

[AU: Ramachandran statistics should be in methods section at the end of the refinement sub-section.]

[AU: Wavelength of data collection, temperature, beamline should all be in methods section.]