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4RHI

Crystal structure of SeMet-labeled wild-type T. brucei arginase-like protein in P321 space group

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X29A
Synchrotron siteNSLS
BeamlineX29A
Temperature [K]100
Detector technologyCCD
Collection date2013-07-23
DetectorADSC QUANTUM 315r
Wavelength(s)0.9788
Spacegroup nameP 3 2 1
Unit cell lengths139.009, 139.009, 90.509
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution42.360 - 2.550
R-factor0.2228
Rwork0.221
R-free0.26060
Structure solution methodSAD
RMSD bond length0.003
RMSD bond angle0.628
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareHKL2Map
Refinement softwarePHENIX ((phenix.refine: 1.8.3_1479))
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]50.00050.0002.640
High resolution limit [Å]2.5505.4902.550
Number of reflections33070
Completeness [%]100.099.9100
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP7.42940.1 M HEPES, pH 7.4, 10% PEG 3350, 5% 2-methyl-2,4-pentanediol, VAPOR DIFFUSION, SITTING DROP, temperature 294K

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