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4BVQ

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

Replaces:  3ZGR
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron siteAustralian Synchrotron
BeamlineMX2
Temperature [K]100
Detector technologyCCD
Collection date2012-10-09
DetectorADSC QUANTUM 315
Spacegroup nameH 3 2
Unit cell lengths130.659, 130.659, 236.947
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution43.750 - 1.900
R-factor0.17077
Rwork0.170
R-free0.18929
Structure solution methodSIRAS
Starting model (for MR)NONE
RMSD bond length0.005
RMSD bond angle1.098
Data reduction softwareXDS
Data scaling softwareSCALA
Phasing softwareAuto-Rickshaw
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]43.7002.000
High resolution limit [Å]1.8901.890
Rmerge0.2401.490
Number of reflections61796
<I/σ(I)>18.94.1
Completeness [%]99.798
Redundancy36.718.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
17.7THE PROTEIN WAS CONCENTRATED TO 10MG/ML AND WAS SET UP IN A 50:50 DROP WITH THE RESERVOIR BEING 38% V/V PEG MME 350 AND 100 MM HEPES PH 7.7

220113

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