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. 2010 Nov 30;286(6):4555–4565. doi: 10.1074/jbc.M110.177360

TABLE 2.

Data collection and refinement statistics

Data collection
    Wavelength (Å) 0.9780
    Space group P 3 2 1
    Cell dimensions (Å) a = b = 159.15, c = 146.29
    Resolution range (Å)a 19.9–2.7 (2.85–2.7)
    No. observations 957,586 (62,188)
    No. unique reflections 58,889 (8,535)
    Completeness (%) 99.7 (99.9)
    Multiplicity 16.3 (7.3)
    Mean I/σ(I) 19.6 (2.9)
    Rmerge 0.104 (0.566)
    Rmeasb 0.107 (0.609)
Refinement
    Resolution range (Å) 19.9–2.7
    Number of reflections used 54,832
    Number of protein atoms 8343
    Number of solvent atoms
        Water 152
        Na+ ion 1
    Mean B values (Å2)
        Protein (aniso)c 79.61
        Water (iso) 42.22
        Na+ ion (iso) 73.95
    Root mean square deviations from ideal geometry
        Bond distances (Å) 0.009
        Bond angles (degree) 1.14
    Rcryst/Rfree 0.176/0.224

a Values in parentheses refer to the highest resolution shell.

b Rmeas is the redundancy-independent residual on intensities (49).

c The protein atom positions were refined using TLS-restrained anisotropic refinement. TLS groups for the protein chains were determined using the TLSMD server (34).