3W9A
Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NW12A |
Synchrotron site | Photon Factory |
Beamline | AR-NW12A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-01-27 |
Detector | ADSC QUANTUM 210r |
Wavelength(s) | 0.97905 |
Spacegroup name | P 1 |
Unit cell lengths | 59.200, 68.421, 69.168 |
Unit cell angles | 89.99, 72.87, 85.81 |
Refinement procedure
Resolution | 30.040 - 1.990 |
R-factor | 0.19089 |
Rwork | 0.188 |
R-free | 0.23587 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.270 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.040 | 2.070 |
High resolution limit [Å] | 1.986 | 2.000 |
Rmerge | 0.105 | 0.289 |
Number of reflections | 66894 | |
Completeness [%] | 94.7 | 88.2 |
Redundancy | 4.2 | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 7% PEG4000, 100mM ammonium sulfate, 100mM sodium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |