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. Author manuscript; available in PMC: 2012 Jun 4.
Published in final edited form as: Structure. 2000 May 15;8(5):505–514. doi: 10.1016/s0969-2126(00)00134-9

Table 2.

Refinement statistics.

Crystal CynSeMet CynSeMet-Oxl
Resolution range (Å) 20–1.65 20–1.65
R factor (%) 15.0 13.9
Rfree (%) 18.9 17.8
No. of protein atoms (including double conformations) 12,230 12,184
No. solvent atoms 1865 2464
Rms deviations from ideal geometry
    bond distance (1–2) (Å) 0.018 (0.02) 0.017 (0.02)*
    angle distance (1–3) (Å) 0.033 (0.04) 0.031 (0.04)
    planar distance (1–4) (Å) 0.038 0.035 (0.05)
Mean B factors (Å2)
    all atoms 17.9 15.9
    protein atoms 15.7 13.1
    water 30.4 28.6
    chloride ions 15.8 –
    sulfate ions 44.7 38.4
    oxalate ions – 13.6
Ramachandran plot statistics
    most favored regions (%) 95.1 94.6
    additional allowed regions (%) 4.2 4.7
    disallowed regions (%) 0.7 (Arg87) 0.7 (Arg87)
Cruickshank diffraction-component precision index (DPI) 0.089 0.078

CynSeMet, selenomethionine-labeled cyanase; CynSeMet-Oxl, CynSeMet soaked with oxalate.

*

Target values.