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2C99

Structural basis of the nucleotide driven conformational changes in the AAA domain of transcription activator PspF

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]100
Detector technologyCCD
Collection date2004-11-27
DetectorADSC CCD
Spacegroup nameP 65
Unit cell lengths113.250, 113.250, 39.332
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution100.000 - 1.900
R-factor0.166
Rwork0.164
R-free0.21200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)2bjw
RMSD bond length0.021
RMSD bond angle1.951
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareREFMAC (5.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]100.0001.970
High resolution limit [Å]1.9001.900
Rmerge0.0500.320
Number of reflections22409
<I/σ(I)>22.72.9
Completeness [%]97.692.4
Redundancy63.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
182M AMMONIUM FORMATE, 0.1 M HEPES PH 8.0, 5% MPD

219869

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