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4F5F

Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU300
Temperature [K]85
Detector technologyCCD
Collection date2010-08-18
DetectorBRUKER SMART 6000
Wavelength(s)1.54
Spacegroup nameP 21 21 21
Unit cell lengths60.189, 103.685, 138.904
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution57.703 - 2.250
R-factor0.1761
Rwork0.174
R-free0.21330
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007
RMSD bond angle1.045
Data reduction softwarePROTEUM PLUS (PLUS)
Data scaling softwarePROTEUM PLUS (PLUS)
Phasing softwarePHASER
Refinement softwarePHENIX ((phenix.refine: 1.7.1_743))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]57.7032.340
High resolution limit [Å]2.2502.250
Rmerge0.0870.325
Number of reflections41556
<I/σ(I)>12.832.53
Completeness [%]98.687.5
Redundancy4.912.35
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP52778% PEG 4000, 0.1 M Sodium Acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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