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1YE9

Crystal structure of proteolytically truncated catalase HPII from E. coli

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-3
Synchrotron siteESRF
BeamlineID14-3
Temperature [K]100
Detector technologyCCD
Collection date2003-09-18
DetectorMARRESEARCH
Wavelength(s)0.931
Spacegroup nameP 1 21 1
Unit cell lengths111.011, 152.888, 135.287
Unit cell angles90.00, 97.54, 90.00
Refinement procedure
Resolution30.000 - 2.800
R-factor0.21977
Rwork0.217
R-free0.26902
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1gge
RMSD bond length0.015
RMSD bond angle2.048
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareMOLREP
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.870
High resolution limit [Å]2.8002.800
Rmerge0.070
Number of reflections104927
<I/σ(I)>6.61
Completeness [%]95.492.1
Redundancy3.33
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP729850mM TrisHCl, 8% PEG 20000, 8% PEG MME 550, 0.2M KSCN, 0.1M dithiothreitol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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