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4AZJ

Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsMAX II BEAMLINE I711
Synchrotron siteMAX II
BeamlineI711
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2003-02-05
DetectorMARRESEARCH
Spacegroup nameC 2 2 21
Unit cell lengths104.692, 136.194, 151.283
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution19.876 - 1.500
R-factor0.1466
Rwork0.146
R-free0.16480
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1w23
RMSD bond length0.012
RMSD bond angle1.464
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwarePHENIX ((PHENIX.REFINE: 1.7.2_869))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.540
High resolution limit [Å]1.5001.500
Rmerge0.0600.330
Number of reflections170566
<I/σ(I)>132.2
Completeness [%]99.499.5
Redundancy4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
18.51.4 M TRI-SODIUM CITRATE, 0.1 M TRIS-HCL, PH 8.5. C0-CRYSTALLIZATION WITH 25 MM L-PHOSPHOSERINE

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