Table 1

Data collection and refinement statistics for the CHS F215S mutant

Resolution, Å26.0–1.63
Total reflections/unique reflections226,775/43,804 
Completeness of data (highest shell), %95.9 (81.6)
I/σ (highest shell)27.5 (6.1)
Rsym* (highest shell), %3.5 (12.0)
Rcryst/Rfree, %19.0/22.5
No. of protein atoms3,108
No. of water molecules347
Rmsd–ideal bond lengths, Å0.013
Rmsd–ideal bond angles, deg2.1
Avg. B-factor–protein, Å218.5
Avg. B-factor–solvent, Å228.8
  • * Rsym = ∑|Ih − 〈Ih〉|/∑Ih, where 〈Ih〉 is the average intensity over symmetry equivalent reflections. 

  • Rcryst = ∑|FobsFcalc|/∑Fobs, where summation is over the data used for refinement. 

  • Rfree is the same definition as for Rcryst, but includes only 5% of data excluded from refinement.