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1C9S

CRYSTAL STRUCTURE OF A COMPLEX OF TRP RNA-BINDING ATTENUATION PROTEIN WITH A 53-BASE SINGLE STRANDED RNA CONTAINING ELEVEN GAG TRIPLETS SEPARATED BY AU DINUCLEOTIDES

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron siteEMBL/DESY, HAMBURG
BeamlineBW7B
Temperature [K]120
Detector technologyIMAGE PLATE
Collection date1997-10-25
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths150.970, 111.670, 138.680
Unit cell angles90.00, 117.77, 90.00
Refinement procedure
Resolution30.000 - 1.900
R-factor0.188

*

Rwork0.188
R-free0.23500
RMSD bond length0.010

*

RMSD bond angle0.026

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareAMoRE
Refinement softwareREFMAC
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.930
High resolution limit [Å]1.9001.900
Rmerge0.0880.396
Number of reflections154404

*

<I/σ(I)>11.8
Completeness [%]96.471.7
Redundancy3.32.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP7.8293PEG 2000 MONOMETHYL ETHER, TRIETHANOLAMINE, MGCL2, K-GLUTAMATE, K-PHOSPHATE, L- TRYPTOPHAN, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein15 (mg/ml)
21droppotassium phosphate50 (mM)
31dropL-tryptophan7.5 (mM)
41reservoirpotassium glutamate0.2 (M)
51reservoirtriethanolamine50 (mM)
61reservoir10 (mM)
71reservoirmPEG20009-12 (%)

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