4E51

Crystal structure of a histidyl-tRNA synthetase HisRS from Burkholderia thailandensis bound to histidine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2012-02-25
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.976484
Spacegroup name	P 21 21 21
Unit cell lengths	70.160, 116.360, 142.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.610 - 2.650
R-factor	0.2078
Rwork	0.206
R-free	0.24040
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1htt
RMSD bond length	0.012
RMSD bond angle	1.464
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	50.000	2.720
High resolution limit [Å]	2.650	11.850	2.650
Rmerge	0.065	0.027	0.524
Number of reflections	34582	348	2541
<I/σ(I)>	24.34	59.64	4.22
Completeness [%]	99.5	76.3	99.9
Redundancy	7.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	ButhA.00063.a.A1 PS01164 at 31 mg/mL with 5 mM L-histidine against Wizard III A3 focus screen, 350 mM magnesium formate, 12% PEG 3350 with 20% glycerol as cryo-protectant, crystal tracking ID 230808g3, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K