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Table 1 X-ray data collection, phasing and refinement statistics

From: Crystal structure of the signaling helix coiled-coil domain of the β1 subunit of the soluble guanylyl cyclase

Data collection Se-Peak
Wavelength (Å) 0.97926
Space group C2
Cell dimension a = 152.039 Å
  b = 65.814 Å
  c = 98.626 Å
  β = 129.948°
Resolution (Å) 50.0-2.15 (2.23-2.15)
Total observations 298063
Unique observations 78615
I/SigI 10.9 (2.1)
Redundancy 3.8 (3.8)
Completeness 99.2 (99.5)
Rsyma (%) 8.2 (34.6)
SAD phasing  
Resolution 50.0-2.2
No. of Se sitesb 14
FOMSOLVEc 0.3
FOMRESOLVEd 0.64
Refinement  
Resolution (Å) 50.0-2.15
No. of protein atoms 4152
No. of waters 460
Rwork (%) 21.3
Rfree(%) 26.1
RMSD bond length (Å) 0.010
RMSD bond angles (°) 1.21
Ramachandran plot  
Most favoured (%) 98.3
Additionally allowed (%) 1.5
Generously allowed (%) 0.2
Disallowed (%) 0.0
  1. Values in parentheses represent the highest resolution shell
  2. aRsym(I) = Σ hkl Σ i |I i (hkl) - I(hkl)|/Σ hkl Σ i I i (hkl) where the summations are over i observations of each reflections and all hkl. I(hkl) is the average intensity of the i observations. Rwork = |F(obs)-F(calc)|/F(obs)
  3. bNumber of selenium sites located by SOLVE
  4. cFigure of merit calculated from SOLVE
  5. dFigure of merit calculated from RESOLVE
  6. eRfree is calculated for 5% of randomly selected reflections not used in the refinement