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. Author manuscript; available in PMC: 2015 Jan 7.
Published in final edited form as: Structure. 2013 Nov 14;22(1):116–124. doi: 10.1016/j.str.2013.09.021

Table 1.

Data and refinement statistics.

Apo cGMP bound High-resolution cGMP-Bound (Iodine SAD)
Data collection
Wavelength (Å) 0.97931 0.97931 1.54178
Space group P3121 P41212 P41212
Cell dimensions
a,b,c (Å) 78.8,78.8,147.6 47.2, 47.2,101.9 47.9,47.9,104.1
α,β,γ (°) 90,90,120 90,90,90 90,90,90
Resolution (Å) 36.9-2.00 23.8-1.65 15.0-1.80
Rsym or Rmerge 11.4(45.1)* 7.7(47.1) 6.0(21.4)
I/σI 10.2(3.4) 20.1(5.5) 32.2/(2.1)
Completeness (%) 99.4(96.4) 99.6(100) 91.2(35.7)
Redundancy 4.8(4.4) 13.5(13.8) 7.2(5.9)
Refinement
Resolution (Å) 36.9 – 2.00 23.8 – 1.65 15.0 – 1.80
No. reflections 36516 14492 19090
Rwork/Rfree 18.82/22.69 19.74/24.47 18.9/24.4
No. atoms
 Proteins 2934 985 985
 Ligand/ion 14 46 45
 Water 343 68 56
B-factors
 Protein 46.424 28.464 37.069
 Ligand/ion 83.734 32.253 49.169
 Water 45.140 38.431 37.139
R.m.s. deviations
 Bond lengths (Å) 0.006 0.006 0.007
 Bond angles (°) 0.980 1.093 1.149
*

Highest resolution shell is shown in parenthesis.

5.0% of the observed intensities was excluded from refinement for cross validation purposes.