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2HZP

Crystal Structure of Homo Sapiens Kynureninase

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-BM
Synchrotron siteAPS
Beamline19-BM
Temperature [K]100
Detector technologyCCD
Collection date2004-06-12
DetectorMARRESEARCH
Wavelength(s)0.97934
Spacegroup nameC 1 2 1
Unit cell lengths74.117, 76.838, 93.274
Unit cell angles90.00, 108.70, 90.00
Refinement procedure
Resolution88.390 - 2.000
R-factor0.15217
Rwork0.150
R-free0.19534
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1qz9
RMSD bond length0.008
RMSD bond angle1.135
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.2.0019)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]88.3902.080
High resolution limit [Å]2.0002.000
Rmerge0.0550.264
Number of reflections33266
<I/σ(I)>24.685.046
Completeness [%]99.898.8
Redundancy3.73.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Microbatch under oil8298A 9.2 mg/ml kynureninase solution in 50 mM HEPES pH 5.2, 0.2 mM PLP was mixed in equal parts with 0.1 M Tris-Cl pH 8.0, 0.05 M MgCl2, 25% PEG 3000, Microbatch under oil, temperature 298K

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