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4LGX

Structure of Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE BM14
Synchrotron siteESRF
BeamlineBM14
Temperature [K]77
Detector technologyCCD
Collection date2013-04-21
DetectorMARRESEARCH
Wavelength(s)0.97
Spacegroup nameP 21 21 2
Unit cell lengths75.330, 87.156, 59.546
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution35.190 - 1.490
R-factor0.1631
Rwork0.162
R-free0.17649
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3qok
RMSD bond length0.016
RMSD bond angle1.627
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.5.0109)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]35.1901.520
High resolution limit [Å]1.4901.490
Number of reflections64748
<I/σ(I)>44.56.1
Completeness [%]100.0100
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4.62982M SODIUM FORMATE, 0.1M SODIUM ACETATE, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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