Skip to main content

Advertisement

Table 1 X-Ray Data Processing and Refinement Statistics

From: Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site

  ybgI native ybgI SeMet
diffraction data     
space group P3 P3
cell (a,b,c) (Å) 156.7,156.7,57.6 154.7,154.7,57.5
resolution (Å) 2.2 2.2
wavelength (Å) 0.9795 0.9793 0.9795 0.9780
no. measured intensities 303,926 298,729 298,987 297,849
no. unique reflection 80,094 77,951 77,981 77,584
mean redundancy 5 2 2 2
R merge (all/high res.) 0.096/0.237 0.056/0.199 0.060/0.216 0.053/0.190
completeness (all/high res.) 99.8/99.6 97.7/86.7 97.6/86.3 97.8/88.8
I/s average (all/high res.) 14.1/2.8 24.3/3.8 23.7/3.5 25.6/4.2
Refinement     
resolution limits used (Å) 20.0-2.2 20.0-2.2
R-factor (95% data) 0.213 0.213
Rfree (5% data) 0.252 0.260
amino acid residues/atoms 1482/11382 1482/11382
non-protein atoms 11 Mg ions 12 Fe ions
no. of water molecules 576 637
bond length rms deviation (Å) 0.026 0.025
angle rms deviation (°) 2.2 2.4
average B (main/side chain) (Å2) 15.3/16.5 18.3/19.1
average B water (Å2) 20.4 24.4