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3SC7

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM30A
Synchrotron siteESRF
BeamlineBM30A
Temperature [K]100
Detector technologyCCD
Collection date2009-11-23
DetectorMARRESEARCH
Wavelength(s)0.9797
Spacegroup nameP 31 2 1
Unit cell lengths95.090, 95.090, 130.560
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution47.570 - 1.500
R-factor0.19054
Rwork0.189
R-free0.21064
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.010
RMSD bond angle1.512
Data reduction softwareXDS
Data scaling softwareXSCALE
Phasing softwarePHASER
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]47.5701.590
High resolution limit [Å]1.5001.500
Rmerge0.054
Number of reflections108977
Completeness [%]94.184.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.52980.1 M HEPES pH 7.5, 1.4 M K-Na tartrate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

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