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1Y39

Co-evolution of protein and RNA structures within a highly conserved ribosomal domain

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSRS BEAMLINE PX9.6
Synchrotron siteSRS
BeamlinePX9.6
Temperature [K]200
Detector technologyCCD
Collection date2004-05-08
DetectorADSC QUANTUM 4
Wavelength(s)0.87
Spacegroup nameP 43 21 2
Unit cell lengths150.240, 150.240, 62.984
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution18.000 - 2.800
R-factor0.22
Rwork0.220
R-free0.25300
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1hc8
RMSD bond length0.006
RMSD bond angle1.100
Data reduction softwareMOSFLM
Data scaling softwareCCP4 ((SCALA))
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]18.0002.900
High resolution limit [Å]2.8002.800
Rmerge0.0610.445
Number of reflections177641744
<I/σ(I)>185.1
Completeness [%]97.598.1
Redundancy4.84.9
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6.5310PEG600, Magnesium acetate, glycerol, sodium cacodylate, potasium chlroride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Crystallization Reagents
IDcrystal IDsolution IDreagent nameconcentrationdetails
111PEG600
1012potasium chlroride
211Magnesium acetate
311glycerol
411sodium cacodylate
511potasium chlroride
612PEG600
712Magnesium acetate
812glycerol
912sodium cacodylate

246031

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