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Table 2 Data collection and refinement statistics of XacAbf51 crystal structure

From: The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans

Data collection
 Space group P21
 Cell dimensions
  a, b, c (Å) 91.34, 163.23, 114.42
  β (º) 107.57
  Resolution (Å) 48.74–1.91 (2.03–1.91)
  Rmeas 0.113 (0.639)
  II 9.74 (2.06)
  Completeness (%) 95.1 (80.3)
  Redundancy 3.4 (2.8)
  CC ½ 99.6 (72.9)
  1. Values in parentheses are for highest resolution shell
  2. aRamachandran data were calculated using MolProbity
Refinement
 Resolution (Å) 48.74–1.91
 No. of reflections 234,093
 Rwork/Rfree 0.149/0.167
 Protein residues 2964 (6 chains)
 Ligands 6 GOL
 Water 2384
 B-factors (Å2)
  Average 24.64
  Protein 24.00
  Ligand 23.05
  Water 30.75
 R.m.s. deviations
  Bond lengths (Å) 0.0116
  Bond angles (°) 1.5092
Ramachandrana
 Favored (%) 97
 Allowed (%) 3
 Outliers (%) 0
 MolProbity score 1.00
 PDB code 6D25
  1. Values in parentheses are for highest resolution shell
  2. aRamachandran data were calculated using MolProbity