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1US2

Xylanase10C (mutant E385A) from Cellvibrio japonicus in complex with xylopentaose

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]100
Detector technologyCCD
Collection date2001-05-15
DetectorADSC QUANTUM 4
Spacegroup nameP 21 21 21
Unit cell lengths44.597, 82.686, 170.727
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000

*

- 1.850
R-factor0.181
Rwork0.179
R-free0.23000

*

Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1clx
RMSD bond length0.017
RMSD bond angle1.400

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.920
High resolution limit [Å]1.8501.850
Rmerge0.0800.370
Number of reflections53227
<I/σ(I)>18.54.8
Completeness [%]98.098
Redundancy4.44.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

718

*

30 MG/ML PROTEIN 0.2 M SODIUM IODIDE, 20% PEG 3350, 20 MM (1 UL) XYLOPENTAOSE, pH 7.00
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein30 (mg/ml)
21reservoirsodium iodide0.2 (M)
31reservoirPEG335020 (%(w/v))
41reservoirxylopentaose20 (mM)

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PDB entries from 2024-05-15

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