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1TOH

TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT

Experimental procedure
Source typeSYNCHROTRON
Source detailsSSRL BEAMLINE BL7-1
Synchrotron siteSSRL
BeamlineBL7-1
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-06
DetectorMARRESEARCH
Spacegroup nameF 2 2 2
Unit cell lengths189.323, 148.335, 57.975
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution37.000 - 2.300
R-factor0.2109
Rwork0.211
R-free0.26800
Structure solution methodMIRAS
RMSD bond length0.019
RMSD bond angle22.800

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS (0.3)
Refinement softwareCNS (0.3)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.380
High resolution limit [Å]2.3002.300
Rmerge0.0420.187
Total number of observations126857

*

Number of reflections18068
<I/σ(I)>21.35
Completeness [%]98.092
Redundancy75.5
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Microdialysis

*

7.94

*

1.2 M AMMONIUM SULFATE 3.2% PEG 200 5% GLYCEROL 2 MM DTT 80 MM TRIS, PH 7.9 CRYSTALS GROWN AT 4 DEGREES C, temperature 277K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein8 (mg/ml)
1012dithiothreitol2 (mM)
211ammonium sulfate120 (mM)
311Tris-HCl100 (mM)
411glycerol5 (%)
511dithiothreitol2 (mM)
612ammonium sulfate1.15 (M)
712PEG2003.2 (%)
812glycerol5 (%)
912Tris-HCl80 (mM)

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