Table 1

Crystallographic statistics
Cap32/34
Data Collection
Space Group P41
Cell Dimensions
  a, b, c (Å) 124.5, 124.5, 77.5
  α, β, γ (º) 90, 90, 90
Resolution Range (Å) 50-2.2 (2.3-2.2)
Number of Reflections 367874
Number of Unique Reflections 60185
Completeness (%) 99.8 (99.6)
Multiplicity
Rmerge 14.9 (83.5)
<I/σI> 14.2 (3.8)
Refinement
Rwork 0.226
Rfree§ 0.265
R.m.s. deviations
  Bond lengths (Å) 0.008
  Bond angles (°) 1.36
Ramachandran Analysis
  Residues in most favoured regions (%) 95.9
  Residues in allowed regions (%) 4.1
  Outliers (%) 0
Model statistics
Protein residues:
  No. in subunit A & B 514
  B-factor A & B (Å2) 15.4
Additional groups:
  Water (No. / B-factor) 328 / 37.9

Values in parentheses refer to the highest resolution shell.

Rmerge = ΣhklΣi|Ii(hkl) - < I(hkl) > |/ ΣhklΣiIi(hkl); where Ii(hkl) is the intensity of the ith measurement of reflection hkl and < I(hkl) > is the mean value of Ii(hkl) for all i measurements.

Rwork = Σhkl||Fo|-|Fc||/Σ|Fo|,where Fo is the observed structure factor and Fc is the calculated structure factor.

§Rfree is the same as Rcryst except calculated with a subset, 5%, of data that are excluded from refinement calculations.

Eckert et al.

Eckert et al. BMC Structural Biology 2012 12:12   doi:10.1186/1472-6807-12-12

Open Data