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2I2O

Crystal Structure of an eIF4G-like Protein from Danio rerio

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsAPS BEAMLINE 22-ID
Synchrotron siteAPS
Beamline22-ID
Temperature [K]100
Detector technologyCCD
Collection date2006-08-04
DetectorMARMOSAIC 300 mm CCD
Wavelength(s)0.97925
Spacegroup nameC 1 2 1
Unit cell lengths317.796, 40.948, 40.917
Unit cell angles90.00, 90.26, 90.00
Refinement procedure
Resolution40.612 - 1.920
R-factor0.192
Rwork0.190
R-free0.23500
Structure solution methodSAD
RMSD bond length0.015
RMSD bond angle1.357
Data reduction softwareHKL-2000
Data scaling softwareHKL
Phasing softwareSHARP
Refinement softwareREFMAC (5.2.0005)
Data quality characteristics
 OverallInner shellOuter shell
Low resolution limit [Å]40.61240.6101.990
High resolution limit [Å]1.9204.1401.920
Rmerge0.0740.0540.245
Number of reflections39789
<I/σ(I)>13.3775.769
Completeness [%]97.510095.5
Redundancy6.47.15.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP293PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 M BisTris PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (7% PEG 4K, 0.40 M sodium chloride, 0.1 M MES/Acetate pH 5.5) CRYOPROTECTED WITH 10% PEG 4K, 0.1 M MES/Acetate pH 5.5, 25% Ethylene glycol, vapor diffusion, hanging drop, temperature 293K

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