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1DBG

CRYSTAL STRUCTURE OF CHONDROITINASE B

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1998-11-11
DetectorRIGAKU RAXIS II
Spacegroup nameP 1 21 1
Unit cell lengths50.600, 74.400, 58.700
Unit cell angles90.00, 92.90, 90.00
Refinement procedure
Resolution50.000 - 1.700
R-factor0.19
Rwork0.180
R-free0.21000
RMSD bond length0.006
RMSD bond angle1.000
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMLPHARE
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.730
High resolution limit [Å]1.7001.700
Rmerge0.0470.142
Total number of observations241256

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Number of reflections44806

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<I/σ(I)>20
Completeness [%]93.758.5
Redundancy2.91.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.7292

*

Li, Y., (1999) Acta Crystallog. Sect., D55, 1055.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein6-8 (mg/ml)
21reservoirPEG800019 (%(w/v))
31reservoirBicine100 (mM)
41reservoirTris-HCl100 (mM)
51reservoirammonium acetate0.15 (M)
61reservoirMPD15 (%(v/v))

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