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3WT4

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPAL/PLS BEAMLINE 4A
Synchrotron sitePAL/PLS
Beamline4A
Temperature [K]100
Detector technologyCCD
Collection date2008-04-30
DetectorADSC QUANTUM 315r
Wavelength(s)0.99999999
Spacegroup nameH 3
Unit cell lengths134.187, 134.187, 328.756
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution27.400 - 2.300
R-factor0.14854
Rwork0.146
R-free0.19632
Structure solution methodMOLECULAR REPLACEMENT
RMSD bond length0.018
RMSD bond angle1.917
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.7.0029)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.00030.000
High resolution limit [Å]2.3002.300
Rmerge0.1030.103
Number of reflections93254
<I/σ(I)>11.08
Completeness [%]94.999
Redundancy3.43.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION829530% PEG400, 0.1M Tris pH 8.0, 0.2M MgCl2, 0.1mM ZnCl2, VAPOR DIFFUSION, temperature 295K

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