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2OS1

Structures of actinonin bound peptide deformylases from E. faecalis and S. pyogenes

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsPAL/PLS BEAMLINE 6B
Synchrotron sitePAL/PLS
Beamline6B
Temperature [K]100
Detector technologyCCD
Collection date2004-11-26
DetectorBRUKER PROTEUM 300
Wavelength(s)1.12714
Spacegroup nameP 43
Unit cell lengths67.999, 67.999, 41.127
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution24.040 - 1.500
R-factor0.186
Rwork0.186
R-free0.19800
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1lqy
RMSD bond length0.014
RMSD bond angle1.400
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.450
High resolution limit [Å]1.4001.400
Rmerge0.0520.283
Number of reflections37104
<I/σ(I)>28.34.5
Completeness [%]86.419.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.429416% PEG 8000, 0.2M Ammonium sulfate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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