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. 2009 Jul 8;284(36):24185–24191. doi: 10.1074/jbc.M109.029116

TABLE 1.

Data collection and refinement statistics

TS5/Marimastat TS5/Compound 8 TS5/Compound 11 MMP13/Marimastat
Data collection
    Space group P21 P21 P21 P21212
    Cell dimensions 52.61, 44.46, 76.35 (Å) 52.82, 44.49, 76.66 (Å) 52.69, 44.44, 76.46 (Å) 119.83, 93.00, 37.00 (Å)
β = 89.81° β = 90.26° β = 89.81°
    Z 4 4 4 8
    Resolution (Å) 50.0-1.70 (1.76-1.70)a 30.0-1.40 (1.45-1.40)a 50.0-2.02 (2.09-2.02)a 30.0-2.40 (2.49-2.40)a
    Total unique reflections 39599 70352 23516 16839
    Rmerge 0.059 (0.350) 0.060 (0.259) 0.044 (0.098) 0.107 (0.417)
    I/σI 19.4 (2.3) 24.1 (3.3) 29.1 (7.8) 10.4 (2.1)
    Completeness (%) 96.9 (82.3) 99.5 (97.3) 99.8 (98.2) 95.2 (03/5)
    Redundancy 3.4 (2.1) 3.6 (3.3) 3.6 (2.1) 3.8 (3.5)

Refinement
    Resolution (Å) 26.31-1.70 25.55-1.40 26.31-1.70 28.51-2.40
    No. reflections 39569 70344 23500 16834
    Rwork/Rfree 0.173/0.224 0.181/0.210 0.159/0.238 0.196/0.286
    No. non-hydrogen atoms (molecule A/molecule B)
        Protein 1668/1668 1668/1668 1668/1668 1304/1304
        Ligand 23/23 27/27 32/32 23/23
        Ion 4/4 4/4 4/4 6/6
        HEPES
        Sulfate
        Water 284/253 293/294 238/249 189/151
    B-factors (average) (molecule A/molecule B)
        Protein (backbone atoms only) 18.29/17.35 13.88/10.70 19.45/15.54 34.21/35.88
        Ligand 20.84/20.76 14.71/12.82 28.16/26.37 20.84/21.79
        Ion 14.29/13.56 9.88/7.80 14.88/13.57 43.41/49.04
        HEPES
        Sulfate
        Water 35.71/34.18 33.79/28.31 36.23/31.08 40.47/42.22
    R.m.s. deviations
        Bond length (Å) 0.009 0.009 0.010 0.009
        Bond angles (°) 1.2 1.4 1.4 1.2

a Values in parentheses are for highest resolution shell. The data were obtained using one crystal.