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Table 1 Data collection and refinement statistics of the dysferlin inner DysF domain

From: Crystal structures of the human Dysferlin inner DysF domain

Data collection PDB 4CAI PDB 4CAH
Wavelength (Å) 1.037530 0.97718
Space group P212121 P213
Unit-cell parameters   
  a, b, c (Å) 74.5, 77.47, 79.89 75.95, 75.95, 75.95
  α, β, γ (o) 90, 90, 90 90, 90, 90
Resolution range (Å) 50-2.2 (2.27-2.20) 53.7-1.9 (1.94-1.9)
Total number of observation 78153 (6922) 115092 (7574)
Total number unique 24062 (2084) 11803 (760)
Completeness 99.8 (99.9) 100.0 (100.0)
Multiplicity 3.2 (3.3) 9.8 (10)
<I/σ(I)> 12.4 (2.3) 30.5 (3.5)
CC(1/2) 0.976 (0.758) 1.00 (0.847)
Rmerge 0.045 (0.466) 0.044 (0.667)
Solvent content (%) 56.8 53.0
Molecule per ASU 3 1
Wilson B factor (Å2) 42.2 31.05
Refinement   
Resolution range (Å) 44.57-2.2 53.7-1.9
Rwork 0.1858 (0.2457) 0.1775 (0.1932)
Rfree 0.2271 (0.3102) 0.1908 (0.2283)
Reflection, working 22764 11220
Reflection, free 1206 549
Average B factor 61.0 42.0
Rmsd bond angle 1.358 1.76
Rmsd bond length (Å) 0.011 0.015
Ramachandran Analysis   
Preferred region (%) 96.7 95.2
Allowed region (%) 2.4 2.9
Outliers (%) 0.9 1.9
  1. Values in parentheses refer to the highest resolution shell.
  2. Rmerge = Σ (I - < I>) / Σ < I > .
  3. Rwork = Σ (|Fobs |- |Fcalc|)/ Σ|Fobs| for 95% of data. Rfree is the same equation for 5% of the data excluded from refinement.