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 aint | 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 |