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Table 1 Data collection, phasing and refinement statistics

From: Structural characterization of a ribose-5-phosphate isomerase B from the pathogenic fungus Coccidioides immitis

  Iodide Phosphate Malonic acid
Data reduction    
Space group C2 F 222 F 222
Unit-cell parameters a = 103.2 Å, b = 49.9 Å, c = 62.0 Å, β = 108.6° a = 77.7 Å, b = 85.2 Å, c = 96.3 Å a = 77.5 Å, b = 84.4 Å, c = 96.2 Å
Resolution range (Å) 50-1.9 (1.95-1.90) 50-1.8 (1.85-1.80) 50-1.7 (1.74-1.70)
Unique reflections 23,513 (1520) 14,967 (1088) 16,561 (1028)
Rmerge 0.043 (0.286) 0.123 (0.397) 0.044 (0.256)
Mean I/σ(I) 13.9 (2.9) 17.5 (3.0) 34.7 (6.6)
Completeness 98.9% (87.5%) 99.8% (98.7%) 94.5% (80.2%)
Multiplicity 5.8 (2.9) 6.9 (3.9) 9.6 (5.3)
Phasing    
Anomalous Correlation 58% (8%)   
SigAno 1.53 (0.81)   
Iodide Sites 21   
FOM (Phaser EP) 0.53   
Refinement    
Rcryst 0.166 (0.185) 0.150 (0.212) 0.144 (0.156)
Rfree 0.205 (0.242) 0.176 (0.270) 0.175 (0.189)
RMSD bonds (Å) 0.015 0.015 0.012
RMSD angles (°) 1.364 1.288 1.323
Protein Atoms 2415 1198 1210
Waters 213 173 169
Iodide Ions 29 0 0
Mean B-factor (Å2) 18.3 13.2 13.7
Reflections 22,275 (1434) 14,170 (1031) 15,677 (968)
Rfree Reflections 1205 752 832
Validation    
Ramachandran favored 100% 100% 98.7%
Ramachandran outliers 0% 0% 0%
Molprobity score [35] 1.42 (97th percentile) 0.98 (100th) 1.32 (97th)
PDB ID 3QD5 3SDW 3SGW
  1. Rfree = Σh||Fobs| - |Fcalc||/Σh|Fobs|. Values in parenthesis indicate the values for the highest of twenty resolution shells
  2. Rfree was calculated using 5% of the reflections omitted from the refinement [31].