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4BVS

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

Replaces:  3ZGT
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron siteAustralian Synchrotron
BeamlineMX2
Temperature [K]100
Detector technologyCCD
Collection date2012-10-18
DetectorADSC QUANTUM 315
Spacegroup nameH 3 2
Unit cell lengths128.365, 128.365, 228.412
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution42.290 - 2.600
R-factor0.1786
Rwork0.177
R-free0.21572
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)3ZGR
RMSD bond length0.007
RMSD bond angle1.189
Data reduction softwareXDS
Data scaling softwareSCALA
Phasing softwarePHASER
Refinement softwareREFMAC (5.7.0032)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]42.2002.740
High resolution limit [Å]2.6002.600
Rmerge0.1400.780
Number of reflections22546
<I/σ(I)>12.83.3
Completeness [%]99.999.9
Redundancy11.111.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
17.4THE PROTEIN WAS DIALYSED AGAINST HEPES BUFFER WITH MELAMINE AND THE FINAL CONCENTRATION OF PROTEIN WAS 2 MG/ML. THIS COMPLEX WAS SET UP IN A 3:2 RATIO WITH 147 MM NACL, 32% V/V PEG 400 AND 100 MM HEPES PH 7.4.

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