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2OUA

Crystal Structure of Nocardiopsis Protease (NAPase)

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsALS BEAMLINE 8.2.2
Synchrotron siteALS
Beamline8.2.2
Temperature [K]100
Detector technologyCCD
Collection date2005-01-13
DetectorADSC QUANTUM 315
Wavelength(s)0.9795
Spacegroup nameP 32 2 1
Unit cell lengths61.605, 61.605, 184.479
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution46.180 - 1.850
Rwork0.176
R-free0.19990
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)poly-Ala model of TFPA (to be submitted)
RMSD bond length0.005
RMSD bond angle1.400
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]46.180
High resolution limit [Å]1.8501.850
Rmerge0.0970.469
Number of reflections34991
<I/σ(I)>16.663.91
Completeness [%]97.498.7
Redundancy5.45.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP62981.3M ammonium sulfate, 10%(v/v) dioxane, 0.1M MES, pH 6.0, 10mg/ml NAPase, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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