Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING. Corrigendum

The two structures reported in the article by Chin et al. [(2013). Acta Cryst. D69, 352–366] have been further refined and corrected.

The original structures reported in the article by Chin et al. (2013) were incorrectly modeled in the C-terminal region, and contained some notable geometrical deviations. The structures have now been corrected, refined again and validated with MolProbity (Chen et al., 2010). The improved structures have been re-deposited in the PDB with the same PDB codes (mSTING-CTD, 4g3l and mSTING-CTD–c-­di-GMP complex, 4g4d). A corrected Table 1 is given below. The conclusions of the paper are not changed by these corrections.

Table 1
Summary of the crystallographic data for mSTING and the mSTING–c-di-GMP complex

Values in parentheses are for the outermost shell.

	Native	SeMet-mSTING	mSTING–c-di-GMP
Beamline	BL13C1	BL13B1	SP44XU
Wavelength (Å)	0.97622	0.97898	0.99808
Space group	P31	P31	P31
Unit-cell parameters (Å, °)	a = b = 78.619, c = 50.418, α = β = 90, γ = 120	a = b = 78.493, c = 50.409, α = β = 90, γ = 120	a = b = 79.058, c = 49.693, α = β = 90, γ = 120
Resolution range (Å)	30–2.39 (2.48–2.39)	30–2.20 (2.28–2.20)	30–2.36 (2.44–2.36)
Total observations	44542 (4387)	125788 (12546)	41778 (5210)
Unique observations	13794 (1371)	17676 (1767)	14245 (1444)
Multiplicity	3.2 (3.2)	7.1 (7.1)	2.9 (2.9)
Completeness (%)	100 (100)	100 (100)	99.6 (100)
Rmerge† (%)	6.1 (59.5)	6.5 (44.7)	3.9 (41.0)
〈I/σ(I)〉	19.4 (2.3)	23.8 (4.9)	17.4 (2.8)
Rfree test-set size (%)	5	5	5
Refinement statistics
Rcryst‡/Rfree§ (%)	22.5/25.1	19.3/25.1	19.7/26.3
Model content
Protein residues	370	368	352
c-di-GMP molecules	0	0	1
Mg^2+ ions	2	2	0
Waters	205	158	124
Average B factors (Å^2)
Backbone atoms	41.8	43.7	41.8
Side-chain atoms	43.6	45.2	44.6
Water O atoms	52.9	51.3	53.1
c-di-GMP molecules			58.9
Ramachandran plot¶, residues in (%)
Most favourable regions	93.1	97.1	93.3
Additionally allowed regions	0.9	2.9	6.1
Outliers		0	0.6
Rotamer outliers (%)		2.8	0.9
R.m.s.d. from ideal geometry
Bonds (Å)	0.008	0.0077	0.008
Angles (°)	1.50	1.14	1.20

†R_merge = .
‡R_cryst = , where F_calc and F_obs are the calculated and observed structure-factor amplitudes, respectively.
§R_free is the same as R_cryst but for 5.0% of the total reflections chosen at random and omitted from refinement.
¶The percentages of residues located in the most favourable, additionally allowed regions and outliers were calculated using the MolProbity program with the default parameters (Chen et al., 2010).