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. 2014 Mar 10;289(16):11465–11475. doi: 10.1074/jbc.M113.543462

TABLE 1.

Data collection and refinement statistics

Data set ObcA
Ligand-free Oxaloacetate C4-CoA adduct Ligand-free
Peak Edge Remote
Crystal Methylated SeMet Native Native Methylated SeMet Methylated SeMet Methylated SeMet
Wavelength (Å) 0.97935 0.97948 0.97948 0.97935 0.97957 0.97167
Resolution (Å)a 50–2.1 (2.18–2.10) 50–2.0 (2.07–2.00) 50–2.28 (2.36–2.28) 50–2.8 (2.90–2.80) 50–2.8 (2.90–2.80) 50–2.8 (2.90–2.80)
Total reflections 548,745 474,350 311,761 264,040 263,537 267,962
Unique reflections 40,015 49,954 33,093 19,639 19,631 19,912
Multiplicity 13.7 (14.5) 9.5 (9.8) 9.4 (9.4) 13.4 (13.2) 13.4 (13.2) 13.5 (13.1)
R-merge (%) 18.0 (59.3) 12.1 (49.5) 15.0 (94.9) 13.1 (51.4) 12.3 (50.4) 13.5 (62.4)
Completeness (%) 95.9 (99.8) 96.2 (100) 99.6 (98.8) 99.8 (100) 99.7 (100) 99.9 (100)
Mean I/sigma (I) 12.1 (5.0) 13.3 (4.7) 11.4 (2.8) 21.4 (5.7) 24.2 (6.1) 22.2 (4.9)
Wilson B-factor 27.65 30.56 32.93
Space group P43212 P43212 P43212 P43212 P43212 P43212

Unit cell (Å)
    a = b, c 173.5, 46.2 177.0, 47.8 174.6, 46.1 178.2, 48.2 178.2, 48.2 178.2, 48.2
    α = β = γ 90 90 90 90 90 90

Refinement
    Rwork (%)b 19.8 21.0 20.2
    Rfree (%)c 23.7 24.6 23.5
    No. of atoms 4270 4056 3937
        Macromolecules 3867 3741 3731
        Ligands 1 10 62
        Water 402 305 144
    Protein residuesd 498 484 483
        Root mean square (bonds) 0.007 0.007 0.008
        Root mean square (angles) 1.08 1.09 1.13
        Ramachandran favored (%) 97 96 96
        Ramachandran outliers (%)e 0 0 0.21
        Clashscore 2.45 2.93 2.78
    Average B-factor 29.8 35.5 32.4
        Macromolecules 29.3 35.3 32.1
        Ligands 19.1 30.5 50.0
        Solvent 34.7 38.2 31.8

a The numbers in parentheses refer to data in the highest resolution shell.

b Rwork = Σ||Fobs| − k|Fcal||/Σ|Fobs|.

c Rfree is the same as Robs for a selected subset (10%) of the reflections that was not included in prior refinement calculations.

d Ordered residues: ligand-free structure (Thr2–Ile70 and Arg92–Arg95 and His101–Ile525), oxaloacetate bound structure (Thr2–Ile70 and Ala111–Ile525), and a C4-CoA adduct bound structure (Thr2–Ile70 and Ala110–Ala523).

e Two outliers identified in C4-CoA adduct bound complex: Ser358 and Gly450.