Skip to main content
. 2015 Sep 30;290(47):28374–28387. doi: 10.1074/jbc.M115.674929

TABLE 2.

Summary of data collection and refinement statistics

Values in parentheses correspond to the highest resolution shell.

PslG(31–442) PslG(31–442) + mannose
Data collection
    Beamline NSLS X29 CLS 08ID-1
    Wavelength (Å) 1.075 0.979
    Space group P41212 P41212
    Cell dimensions
    a, b, c (Å) 83.2, 83.2 163.40 83.6, 83.6 163.4
    α, β, γ (degrees) 90, 90, 90 90, 90, 90
    Resolution (Å) 50.00–2.00 (2.07–2.00) 50.00–1.90 (1.97–1.90)
    No. of reflections 1,197,746 563,367
    No. of unique reflections 39,575 46,642
    Redundancy 30.3 (28.7) 12.1 (12.5)
    II 36.8 (6.1) 36.7 (4.8)
    Completeness (%) 100 (100) 100 (100)
    Rmerge (%)a 13.8 (65.6) 10.7 (63.9)

Refinement
    Rwork/Rfreeb 14.9/18.8 15.5/18.7
    No. of atoms
        Protein 3346 3341
        Cadmium 4 4
        Chlorine 1 1
        Ligands 16 52
        Water 387 355
    Average B-factors (Å2)c
        Protein 23.2 27.1
        Cadmium 57.6 51.5
        Chlorine 52.8 65.0
        Ligands 46.8 73.1
        Water 32.7 37.2
    Root mean square deviations
        Bond lengths (Å) 0.007 0.007
        Bond angles (degrees) 1.03 1.12
    Ramachandran plotc
        Total favored (%) 97.3 96.8
        Total allowed (%) 100 100
    Coordinate error (Å)d 0.16 0.16
    Protein Data Bank code 5BX9 5BXA

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

b 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.

c As calculated using MolProbity (81).

d Maximum likelihood-based coordinate error, as determined by PHENIX (39).