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. Author manuscript; available in PMC: 2015 Feb 9.
Published in final edited form as: Nat Struct Mol Biol. 2013 Oct 6;20(11):1298–1303. doi: 10.1038/nsmb.2683

Table 1.

Data collection and refinement statistics (molecular replacement).

mtRNAP elongation complex
Data collectiona
Space group I23
Cell dimensions
 a=b=c (Å) 225.2
Resolution (Å) 39.8–2.65 (2.72–2.65)b
Rsym (%) 12 (229)
I/σI 18.9 (1.7)
Completeness (%) 100.0 (100.0)
Redundancy 20.7 (20.2)
CC (1/2)c (%) 100 (42.5)
Refinement
Resolution (Å) 39.81–2.65
No. reflections 54985
Rwork/Rfree (%) 17.3/20.8
No. atoms
 Protein 7880
 Ligand/ion 1265
 Water 244
B-factors (Å2)
 Protein 94.4
 Ligand/ion 138.1
 Water 83.5
r.m.s deviations
 Bond lengths (Å) 0.010
 Bond angles (°) 1.24
a

Diffraction data were collected at beamline X06SA of the Swiss Light Source, Switzerland and processed with MOSFLM35.

b

Numbers in parenthesis refer to the highest resolution shell.

c

CC1/2 = percentage of correlation between intensities from random half-datasets36.