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. 2010 May 4;285(27):21060–21069. doi: 10.1074/jbc.M110.119412

TABLE 2.

Structure refinement statistics for H. pylori FlhAC

Statistics
Structure refinement 30.0-2.40 Å (2.462-2.400)a
No. of reflections in working set 19,217 (1,390)a
No. of reflections in test set 1,037 (82)a
Rworkb 0.224 (0.262)a
Rfreec 0.263 (0.315)a
No. of amino acid residues 361
No. of water molecules 70
No. of ligands 0
Average B-factor (Å2)d 26.2
R.m.s. deviation B bonded MC atoms (Å2)d 0.715
R.m.s. deviation B bonded SC atoms (Å2)d 1.36
Rmsd B angle MC atoms (Å2)d 2.16
Rmsd B angle SC atoms (Å2)d 3.40
R.m.s. deviation bond lengths (Å)d 0.011
R.m.s. deviation angles (°)d 1.24
Residues in preferred Ramachandran regions (%)e 91.7
Residues in allowed regions (%)e 8.3

a Values in parentheses correspond to the highest resolution shell.

b Rwork = Σhkl‖Fobs(hkl)‖−|Fcalc(hkl)‖/Σhkl|Fobs(hkl)|, where |Fobs(hkl)| and |Fcalc(hkl)| are the observed and calculated amplitudes, respectively, for the structure factor F(hkl).

c Rfree is the equivalent of Rwork for 5% of the reflections (randomly selected), which were not used in structure refinement.

d B-factor and r.m.s. deviation values were calculated with Refmac as implemented in CCP4 (43–45).

e The Ramachandran plot was generated with Procheck in CCP4 (see supplemental Fig. S3) (45, 53).