Skip to main content
. 2013 Jun 18;288(31):22299–22314. doi: 10.1074/jbc.M113.484931

TABLE 1.

Summary of data collection and refinement statistics

Native SeMet-SAD
Data collection
    Beamline NSLS X29 NSLS X29
    Wavelength (Å) 1.075 0.979
    Space group P21212 P21
    Cell dimensions
        a, b, c (Å) 123.7, 82.4, 92.7 46.4, 121.4, 92.1
        α, β, γ (°) 90.0, 90.0, 90.0 90.0, 95.2, 90.0
    Total no. of reflections 506,683 437,204
    No. of unique reflections 52,314 68,397
    Resolution (Å) 50.0–2.15 (2.23–2.15)a 43.22–2.00 (2.07–2.02)
    Average II 44.7 (4.0) 23.0 (2.1)
    Completeness (%) 98.82 (89.26) 90.7 (64.5)
    Redundancy 9.7 (9.8) 7.1 (6.2)
    Rmerge (%)b 8.1 (64.0) 8.3 (68.1)

Refinement
    Rwork/Rfree (%)c 17.60/23.10
    No. of atoms
        Protein 6,504
        Water 372
    Average B-factor (Å2)
        Protein 50.10
        Water 50.20
    RMSDs
        Bond lengths (Å) 0.007
        Bond angles (degrees) 1.040
Ramachandran plotd
    Total favored (%) 97.0
    Total allowed (%) 100
Coordinate error (Å)e 0.24
PDB code 4KNC

a Values in parentheses correspond to highest resolution shell

b Rmerge = ΣΣ|I(k) − 〈I〉|/ΣI(k), where I(k) and 〈I〉 represent the intensity values of the individual measurements and the corresponding mean values. The summation is over all unique measurements.

c Rwork = Σ‖Fo| − k|Fc‖/|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree is the sum extended over a subset of reflections (5%) excluded from all stages of the refinement.

d As calculated using MOLPROBITY (95).

e Maximum likelihood-based coordinate error as determined by PHENIX (41).