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2I9C

Crystal Structure of the Protein RPA1889 from Rhodopseudomonas palustris CGA009

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 19-BM
Synchrotron siteAPS
Beamline19-BM
Temperature [K]100
Detector technologyCCD
Collection date2006-06-09
DetectorSBC-3
Wavelength(s)0.97904
Spacegroup nameP 32 2 1
Unit cell lengths78.022, 78.022, 38.979
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution33.790 - 2.000
R-factor0.17603
Rwork0.175
R-free0.20189
Structure solution methodSAD
RMSD bond length0.020
RMSD bond angle1.605
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareHKL-3000
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]67.5702.020
High resolution limit [Å]2.0002.000
Rmerge0.0660.299
Number of reflections9449
<I/σ(I)>6.83
Completeness [%]99.7100
Redundancy77.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP72935% Tascimate, 10% PEG5000 MME, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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