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2OS3

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 date2005-02-22
DetectorBRUKER PROTEUM 300
Wavelength(s)1.12714
Spacegroup nameP 31 2 1
Unit cell lengths40.557, 40.557, 217.938
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution19.940 - 2.260
R-factor0.205
Rwork0.205
R-free0.27300
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1lqy
RMSD bond length0.005
RMSD bond angle1.200
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwareCNS
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.280
High resolution limit [Å]2.1002.100
Rmerge0.0950.381
Number of reflections13084
<I/σ(I)>26.73
Completeness [%]98.197.7
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.629430% PEG 4000, 0.1M sodium citrate, 0.2M ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 294K

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