3ZTE

Crystal Structure of the TRP RNA-Binding Attenuation Protein (TRAP) from Bacillus Licheniformis.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX14.2
Synchrotron site	SRS
Beamline	PX14.2
Temperature [K]	120
Detector technology	CCD
Collection date	2006-02-15
Detector	ADSC QUANTUM 4r
Spacegroup name	P 41 21 2
Unit cell lengths	145.427, 145.427, 183.071
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.830 - 2.410
R-factor	0.28401
Rwork	0.281
R-free	0.34606
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qaw
RMSD bond length	0.003
RMSD bond angle	0.782
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.5.0110)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.120	0.210
Number of reflections	76452
<I/σ(I)>	12.1	5.1
Completeness [%]	97.4	82.4
Redundancy	5.4	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5	293	PROTEIN WAS IN BUFFER 50 MM OF POTASSIUM PHOSPHATE; CONCENTRATION 14.7 MG/ML, TEMPERATURE 293K; NO L-TRP WAS ADDED. CRYSTALLISATION CONDITIONS: 0.1 M HEPES PH 7.0, 5% (V/V) TASCIMATE PH 7.0, 10% (W/V) PEG5KMME. CRYOPROTECTION: 15%(W/V) PEG5KMME, 10%(V/V) GLYCEROL.