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1HMU

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X8C
Synchrotron siteNSLS
BeamlineX8C
Temperature [K]100
Detector technologyCCD
Collection date1999-02-02
DetectorADSC QUANTUM 4
Spacegroup nameP 43 21 2
Unit cell lengths86.900, 86.900, 192.300
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.000
Rwork0.227
R-free0.26600
RMSD bond length0.006
RMSD bond angle1.340
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.000
High resolution limit [Å]2.0002.000
Rmerge0.0630.302
Total number of observations282695

*

Number of reflections49755
<I/σ(I)>14.3
Completeness [%]98.698.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.5298PEG 3350, sodium acetate, hepes , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG335015 (%(w/v))
21reservoirsodium acetate400 (mM)
31reservoirHEPES100 (mM)

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