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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)

  I/σI

9.74 (2.06)

  Completeness (%)

95.1 (80.3)

  Redundancy

3.4 (2.8)

  CC ½

99.6 (72.9)

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