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. 2016 Apr 26;72(Pt 5):629–640. doi: 10.1107/S2059798316003065

Table 3. X-ray data-collection and structure-refinement statistics for glucose isomerase.

  I222, 295 K I222, 100 K P21212, 295 K P21212, 100 K
Data collection
 X-ray source I02 I02 I02 I02
 Wavelength (Å) 0.9795 0.9795 0.9795 0.9795
 Space group I222 I222 P21212 P21212
 Unit-cell parameters (Å, °) a = 94.07, b = 99.22, c = 103.03, α = β = γ = 90 a = 92.90, b = 98.15, c = 102.70, α = β = γ = 90 a = 83.49, b = 95.02, c = 98.48, α = β = γ = 90 a = 81.63, b = 93.64, c = 97.64, α = β = γ = 90
 Resolution (Å) 2.0 2.0 2.0 2.0
 Mosaicity (°) 0.15 0.55 1.1 1.1
R merge 0.051 (0.086) 0.050 (0.068) 0.060 (0.138) 0.044 (0.103)
 〈I〉/σ(〈I〉) 18.0 (12.9) 18.7 (15.4) 10.4 (5.9) 14.4 (8.6)
 Completeness (%) 99.8 (99.7) 99.8 (99.8) 99.5 (99.6) 99.5 (99.8)
 Multiplicity 4.5 (4.6) 4.4 (4.6) 3.2 (3.3) 3.2 (3.3)
Refinement
 No. of unique reflections 30438 31979 50546 50965
R cryst 0.106 0.116 0.137 0.136
R free 0.140 0.156 0.180 0.182
 No. of residues
  Protein 387 388 776 776
  Ligands 4 3 14 19
  Water 301 518 446 542
 Average B factors (Å2)
  Protein 17.86 8.54 20.38 14.18
  Sugar 18.90 6.82 20.98 30.49
  Manganese 11.00 6.44 34.46 28.92
  Waters 29.67 23.51 33.00 26.22
 R.m.s. deviations
  Bond lengths (Å) 0.021 0.023 0.022 0.018
  Bond angles (°) 2.077 2.011 2.371 2.029
 Ramachandran statistics (%)
  Favoured 97.1 97.1 96.5 97.0
  Allowed 2.6 2.6 3.2 2.7
  Outliers 0.3 0.3 0.3 0.3
 PDB code 4zb5 4zb2 4zb0 4zbc