Table 1

Data collection and statistics from the crystallographic analysis.

Data set Native 1 (RAXIS II) Native 2 (X25, NSLS)
Data collection
Resolution (Å)99.0–3.0 99.0–2.2
Total observations89,878 218,815
Unique observations 12,533 31,296
Data coverage (outer shell) 97.8% (96.2%) 99.1% (97.6%)
Rsym (outer shell)*0.066 (0.203)0.039 (0.167)
Refinement
Resolution range (Å) 20.0–2.2
Number of reflections (I > 2σ)29,613
Rworking/Rfree21.8%/27.6%
Number of atoms 3888
Number of water molecules 243
rmsd bond length (Å) 0.006
rmsd bond angles (degrees) 1.343
rmsd Bfactors 3.375
  • * Rsym = ΣhΣi|Ih,iIh|/ΣhΣiIh,i, where Ih is the mean intensity of thei observations of symmetry related reflections ofh.

  • R = Σ|FobsFcalc|/ΣFobs, where Fobs = FP, andFcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections).

  • rmsd in bond lengths and angles are the deviations from ideal values, and the rmsd in Bfactors is calculated between bonded atoms.