3V2I

Structure of a Peptidyl-tRNA hydrolase (PTH) from Burkholderia thailandensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-17
Detector	ADSC QUANTUM 210
Wavelength(s)	0.97
Spacegroup name	I 2 2 2
Unit cell lengths	53.340, 93.580, 106.760
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.650
R-factor	0.1767
Rwork	0.175
R-free	0.20550
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ofv
RMSD bond length	0.010
RMSD bond angle	1.605
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.041	0.014	0.422
Number of reflections	32529	390	2386
<I/σ(I)>	30.89	72.97	4.89
Completeness [%]	99.9	91.3	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	ButhA.17877.a.A1 PS01195 34.03 mg/ml, 1000mM sodium citrate, 100mM cacodylate pH 6.5. 25% ethylene glycol for cryoprotection. , VAPOR DIFFUSION, SITTING DROP, temperature 289K