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. 2020 Mar 5;48(7):3987–3997. doi: 10.1093/nar/gkaa149

Table 1.

Selected crystallographic data and refinement statistics

Unit Cell [abc, Å; αβγ, °] a = 65.7, b = 65.8, c = 82.0
α = 105.9, β= 92.3, γ = 119.9
Space Group P1
Wavelength [Å] 1.000
X-ray Source APS SER-CAT 22-BM
Resolution [Å] (Highest shell) 50.0–3.00 (3.05–3.00)
No. of Reflections [unique] 18 997
Completeness [%] 83.8 (53.1)
Rsyma [%] 10.6 (35.0)
I/(σI) 10.3 (2.4)
Redundancy 1.8 (1.5)
Refinement Summary
Resolution [Å] (Highest shell) 25.69–3.00 (3.05–3.00)
Hfq protomers/DNA base pairs/Unit Cell 12/40
No. of non-solvent atoms/Unit Cell 8055
No. of waters/Unit Cell 59
Rworkb [%] 21.1 (23.4)
Rfreec [%] 26.0 (27.9)
Average B factor [Å2]
 Protein 48.6
 DNA 81.6
RMS deviations
 Bonds [Å] 0.006
 Angles [o] 1.13
Ramachandran analysis [%]
 Favored, allowed, disallowed 94.9, 5.1, 0.0
PDB ID: code 5UK7

a R sym = Σ|I- 〈I〉|/ Σ|I|, where I is the observed intensity and is the average intensity of several symmetry-related observations.

b R work = Σ||Fo|-|Fc||/ Σ|Fo, where Fo and Fc are the observed and calculated structure factors, respectively.

c R free = Σ||Fo|-|Fc||/ Σ|Fo for 5% of the data not used at any stage of the structural refinement.