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1AX4

TRYPTOPHANASE FROM PROTEUS VULGARIS

Experimental procedure
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1994-01
DetectorMARRESEARCH
Spacegroup nameP 21 21 21
Unit cell lengths114.990, 118.230, 153.680
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution18.000 - 2.100
R-factor0.187

*

Rwork0.187
R-free0.22749
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)TYROSINE PHENOL LYASE PDB ENTRY 1TPL
RMSD bond length0.012

*

RMSD bond angle0.030

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]18.0002.170
High resolution limit [Å]2.1002.100
Rmerge0.0980.273
Total number of observations397510

*

Number of reflections117863

*

<I/σ(I)>113.2
Completeness [%]97.697.3
Redundancy3.332.49
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

7.827 % PEG 4000, 0.1 M POTASSIUM PHOSPHATE BUFFER PH 7.8, 0.25 MM PYRIDOXAL 5'-PHOSPHATE, 5MM DTT, 0.1 M CSCL.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPLP0.25 (mM)
21reservoirdithiothreitol5 (mM)
31reservoir0.1 (M)
41reservoirpotassium phosphate0.1 (M)
51reservoirPEG400027 (%)

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