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1E0X

XYLANASE 10A FROM SREPTOMYCES LIVIDANS. XYLOBIOSYL-ENZYME INTERMEDIATE AT 1.65 A

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1997-11-15
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths49.210, 81.060, 72.810
Unit cell angles90.00, 102.79, 90.00
Refinement procedure
Resolution15.000 - 1.650
R-factor0.12

*

Rwork0.126
R-free0.16200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)NATIVE STRUCTURE AT 1.2
RMSD bond length0.012
RMSD bond angle0.028
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]15.0001.710
High resolution limit [Å]1.6501.650
Rmerge0.0330.097
Number of reflections66881
<I/σ(I)>35.612.9
Completeness [%]99.094
Redundancy3.54.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.5PROTEIN WAS CRYSTALLISED WITH 18 % PEG 5000 AS PRECIPITANT, 100MM HEPES PH 7.5 AS BUFFER, 10% ISOPROPANOL, CRYSTAL WERE SOAKED IN PRESENCE OF POWDERED SUBSTRATE FOR 12 HOURS. 15% GLYCEROL WAS ADDED AS CRYOPROTECTANT
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirsodium HEPES0.1 (M)
21reservoirPEG500018 (%(w/v))
31dropprotein30 (mg/ml)
41dropisopropanol10 (%(v/v))

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