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Table 1 Crystallographic statistics

From: Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum

  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
R merge 14.9 (83.5)
<I/σI> 14.2 (3.8)
Refinement  
R work 0.226
R free § 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
  1. Values in parentheses refer to the highest resolution shell.
  2. R merge  = Σ hkl Σ i | I i (hkl) - < I(hkl) > |/ Σ hkl Σ i I i (hkl); where I i (hkl) is the intensity of the i th measurement of reflection hkl and < I(hkl) > is the mean value of I i (hkl) for all i measurements.
  3. R work  = Σ hkl ||F o |-|F c ||/Σ|F o |, where F o is the observed structure factor and F c is the calculated structure factor.
  4. §R free is the same as R cryst except calculated with a subset, 5%, of data that are excluded from refinement calculations.