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2CYJ

Crystal structure of conserved hypothetical protein PH1505 from Pyrococcus horikoshii OT3

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSPRING-8 BEAMLINE BL26B1
Synchrotron siteSPring-8
BeamlineBL26B1
Temperature [K]100
Detector technologyCCD
Collection date2005-04-16
DetectorRIGAKU JUPITER 210
Wavelength(s)1.00
Spacegroup nameP 21 21 21
Unit cell lengths27.761, 45.882, 82.851
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution40.140 - 1.500
Rwork0.179
R-free0.20100
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ihn
RMSD bond length0.007
RMSD bond angle1.500
Data reduction softwareHKL-2000
Data scaling softwareSCALEPACK
Phasing softwarePHASER
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]50.0001.550
High resolution limit [Å]1.5001.500
Number of reflections17325
<I/σ(I)>17.0910.11
Completeness [%]97.983.7
Redundancy4.22.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, SITTING DROP4.62930.2M ammonium sulfate, 0.1M sodium acetate trihydrate(pH 4.6), 23% PEG MME 2000, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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