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 method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1997-10-25
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	150.970, 111.670, 138.680
Unit cell angles	90.00, 117.77, 90.00

Refinement procedure

Resolution	30.000 - 1.900
R-factor	0.188 *
Rwork	0.188
R-free	0.23500
RMSD bond length	0.010 *
RMSD bond angle	0.026 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.088	0.396
Number of reflections	154404 *
<I/σ(I)>	11.8
Completeness [%]	96.4	71.7
Redundancy	3.3	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	293	PEG 2000 MONOMETHYL ETHER, TRIETHANOLAMINE, MGCL2, K-GLUTAMATE, K-PHOSPHATE, L- TRYPTOPHAN, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	potassium phosphate	50 (mM)
3	1	drop	L-tryptophan	7.5 (mM)
4	1	reservoir	potassium glutamate	0.2 (M)
5	1	reservoir	triethanolamine	50 (mM)
6	1	reservoir		10 (mM)
7	1	reservoir	mPEG2000	9-12 (%)