4B5Q
The lytic polysaccharide monooxygenase GH61D structure from the basidiomycota fungus Phanerochaete chrysosporium
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 149.308, 37.521, 79.848 |
Unit cell angles | 90.00, 117.41, 90.00 |
Refinement procedure
Resolution | 70.880 - 1.750 |
R-factor | 0.18758 |
Rwork | 0.186 |
R-free | 0.22290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eii |
RMSD bond length | 0.007 |
RMSD bond angle | 1.165 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.070 | 1.840 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.090 | 0.560 |
Number of reflections | 39420 | |
<I/σ(I)> | 10.9 | 2.1 |
Completeness [%] | 98.5 | 97.5 |
Redundancy | 3.4 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 12MG/ML PROTEIN, WITH EQUAL VOLUME 2.1 M DL-MALIC ACID PH 7.0 USING SITTING DROP CRYSTALLIZATION |