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Table 4 Data collection and structural refinement statistics

From: In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin

  LiPH8 variant A55R/N156E-H239E
PDB code 6A6Q
Data collection
 Wavelength (Å) 0.97934
 Unit cell (a, b, c; α, β, g) (Å; °) 41.2, 99.6, 48.3; 90.0, 113.9, 90.0
 Space group P2 1
 Solvent content (%) 66.29
 Protein chains in AU 1
 Resolution range (Å) 50.00–1.66
 Highest resolution shell (Å) 1.69–1.66
 Unique reflections 40,502
 Redundancy 3.2 (2.6)
 Completeness (%) 97.7 (94.4)
 Rmerge (%) 7.8 (29.6)
 Average I/σ(I) 32.1 (5.1)
 CC (1/2) 98.5 (80.3)
Refinement
 Resolution range (Å) 29.72–1.67
 Rwork (%) 14.2
 Rfree (%) 17.1
 Mean B value (Å2)a 21.2
 RMS deviation bond lengths (Å) 0.016
 RMS deviation bond angles (°) 2.0662
 Number of amino acid residues 351
 Number of water molecules 249
Ramachandran plot
 Most favored regions (%) 97.9
 Additional allowed regions (%) 1.8
 Outliers (%) 0.3
  1. a The mean B value is for both protein atoms and the solvent molecules