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. Author manuscript; available in PMC: 2009 Dec 11.
Published in final edited form as: Proteins. 2002 Aug 1;48(2):427–430. doi: 10.1002/prot.10160

TABLE II.

Crystallographic Statistics

Phasing
    Resolution range Inf Peak h-Remote All
    39–2.4 Å Fried Iso Fried Iso Fried
    Phasing power 3.05 1.91 2.71 1.33 1.74
    FOM 0.45 0.38 0.43 0.30 0.32 0.75
    Density modification, FOM (1.8 Å) 0.96
Refinement
    Resolution range (Å) 39–1.63
    No. of reflections 35198
    σ cutoff 0
    R-value 0.194
    Free R-value 0.214 (4024)
    RMSD from ideal geometry
        Bond length (1–2) (Å) 0.005
        Angle (°) 1.20
        Dihedral (°) 21.9
        Improper (°) 0.84
Mean B-factor (Å2)
        All atoms 18.70
        Protein atoms (2149)
            Protein main chain 16.95
            Protein side chain 15.70
        Formate (3) 12.52
        Mg (2) 8.69
        Glycerol (12) 29.26
        Water (272) 30.76
    Ramachandran plot statistics (%)
        Residues in most favored regions 100
        Residues in additional allowed regions 0.0
        Residues in disallowed region 0.0