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1PQ3

Human Arginase II: Crystal Structure and Physiological Role in Male and Female Sexual Arousal

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE F1
Synchrotron siteCHESS
BeamlineF1
Detector technologyCCD
DetectorADSC QUANTUM 4
Spacegroup nameP 32
Unit cell lengths142.994, 142.994, 127.328
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution30.000 - 2.700
R-factor0.227
Rwork0.227
R-free0.24700
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.007

*

RMSD bond angle1.400

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.000
High resolution limit [Å]2.700
Rmerge0.098

*

0.280

*

Total number of observations404391

*

Number of reflections79653

*

Completeness [%]99.3

*

98.9

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

8.54

*

Tris, Ammonium Sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 8.50
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11droparginase7 (mg/ml)
21dropBEC5 (mM)
31dropBicine50 (mM)pH8.5
41dropTris-HCl0.10 (M)pH8.3-8.5
51dropammonium sulfate3.0 (M)
61reservoirTris-HCl0.10 (M)pH8.3-8.5
71reservoirammonium sulfate3.0 (M)
81reservoirglycerol20 (%(v/v))

221051

PDB entries from 2024-06-12

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