Table 1

Summary of crystallographic analysis

Data collection
 Resolution limit, Å1.5
 Total reflections288,900
 Unique reflections67,186
 Completeness, %93.8
Rsym,* (%)6.7
 Resolution, Å20–1.5
 Number of protein atoms3709
 Number of water molecules402
Rcryst, %19.0
Rfree, %21.1
 Average B, Å214.77
 rmsd bond length, Å0.014
 rmsd bond angles, degrees1.80
  • rmsd, rms deviation. 

  • * Rsym = ΣhΣi|Ih,i − 〈Ih|/Σ|〈Ih|, where I is the scaled intensity of the given reflection h

  • Rcryst = Σh|FohFch|/ΣhFoh, where Foh, and Fch are the observed and calculated structure amplitudes for reflection h

  • Value of Rfree for 10% of randomly selected reflections excluded from the refinement.