Skip to main content

Advertisement

Table 1 X-ray data collection and refinement statistics. Statistics for the highest resolution bin are in parenthesis

From: Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues

Data collection
Space group P 32 2 1
 Unit cell, Å, ° a = 77.23, b = 77.23, c = 66.753 β = 122.35
 Wavelength, Å 1.54178
 Temperature (K) 100
 Resolution, Å 25.0–1.99 (2.09–1.99)
 Unique reflections 28,968 (3560)
 R int a 0.155 (0.622)
 Average redundancy 11.9 (3.4)
 <I >/<σ(I)> 10.6 (1.4)
 Completeness,  % 97.9 (90.1)
Refinement
 Resolution, Å 25–2.0 (2.05–2.0)
 R/R free 0.164 (0.302)/0.229 (0.306)
 Protein atoms 3126
 Water molecules 367
 Other atoms 42
 RMSD from ideal bond length, Åb 0.016
 RMSD from ideal bond angles, °b 1.648
 Wilson B-factor 4.8
 Average B-factor for protein atoms, Å2 21.8
 Average B-factor for water molecules, Å2 29.2
Ramachandran plot statistics, %c
 Allowed 100%
 Favored 97.1%
 Outliers 0
  1. aRint = ∑| I – < I>|/∑|I| where I is the intensity of an individual reflection and < I > is the mean intensity of a group of equivalents and the sums are calculated over all reflections with more than one equivalent measured
  2. b[27]
  3. c[26]