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3W9A

Crystal structure of the catalytic domain of the glycoside hydrolase family 131 protein from Coprinopsis cinerea

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPHOTON FACTORY BEAMLINE AR-NW12A
Synchrotron sitePhoton Factory
BeamlineAR-NW12A
Temperature [K]100
Detector technologyCCD
Collection date2010-01-27
DetectorADSC QUANTUM 210r
Wavelength(s)0.97905
Spacegroup nameP 1
Unit cell lengths59.200, 68.421, 69.168
Unit cell angles89.99, 72.87, 85.81
Refinement procedure
Resolution30.040 - 1.990
R-factor0.19089
Rwork0.188
R-free0.23587
Structure solution methodSAD
RMSD bond length0.009
RMSD bond angle1.270
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareAutoSol
Refinement softwareREFMAC (5.7.0029)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0402.070
High resolution limit [Å]1.9862.000
Rmerge0.1050.289
Number of reflections66894
Completeness [%]94.788.2
Redundancy4.24
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP62937% PEG4000, 100mM ammonium sulfate, 100mM sodium phosphate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K

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