4EX5

Crystal structure of lysyl-tRNA synthetase LysRS from Burkholderia thailandensis bound to lysine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2012-04-19
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	86.220, 118.540, 94.540
Unit cell angles	90.00, 113.23, 90.00

Refinement procedure

Resolution	50.000 - 2.400
R-factor	0.1909
Rwork	0.189
R-free	0.22280
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bbu
RMSD bond length	0.012
RMSD bond angle	1.444
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		2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.080	0.025	0.468
Number of reflections	67117	728	4821
<I/σ(I)>	10.87	36.89	2.27
Completeness [%]	98.1	89.9	96.1
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	ButhA.00612.a.A1 PS01208 at 18.9 mg/mL against Morpheus H5, 10% PEG 20,000, 20% PEG 550 MME, 0.1 M MOPS/Hepes, 20 mM glutamate, 20 mM alanine, 20 mM glycine, 20 mM serine, 20 mM lysine, crystal tracking ID 232983h5, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K