Sulfur denitrosylation by an engineered Trx-like DsbG enzyme identifies nucleophilic cysteine hydrogen bonds as key functional determinant. [Additions and Corrections]

VOLUME 291 (2016) PAGES 15020–15028Table 2 was inadvertently omitted in the version of this article that was published on July 15, 2016. This error has now been corrected.jbc;292/46/18831/T2T1T2Table 2X-ray data collection, processing, and refinement statisticsDsbGCGPCDsbGCGPC-T200MData collection    BeamlineProxima IProxima I    Wavelength (Å)0.980110.98011    Space groupC2C2    Unit cella = 116.65, b = 57.03, and c = 85.55 Å; β = 95.14 and α = γ = 90°a = 116.92, b = 57.22, and c =86.04; β = 94.75 and α = γ = 90°    Resolution limits (Å)a46.12–1.70 (1.80–1.70)46.44–1.96 (2.00–1.96)    Total no. of reflections201,432 (26,100)150,037 (8488)    No. of unique reflections61,470 (9506)40,644 (2344)    Completeness99.5 (98.2)99.4 (99.9)    Rmerge0.051 (0.425)0.063 (0.442)    〈I/σ(I)〉16.73 (2.80)15.58 (3.53)    Rcrystb16.8219.16    Rfreec19.2324.08Ramachandran profile    Most favored (%)98.2598.57    Additionally allowed (%)1.000.71    Disallowed (%)0.750.72R.m.s. deviations    Bond lengths (Å)0.0070.007    Bond angles0.972°0.900°    PDB entry5G1L5G1Ka Data in brackets are for the highest resolution shell.b Rcryst = S||Fobs| − |Fcalc||/S|/Fobs|, Fobs and Fcalc are observed and calculated structure factor amplitudes.c Rfree as for Rcryst using a random subset of the data excluded from the refinement.

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