2O5R

Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-08-11
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.94926, 0.97925, 0.97939
Spacegroup name	P 31 2 1
Unit cell lengths	69.953, 69.953, 283.945
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.351 - 2.340
R-factor	0.236
Rwork	0.234
R-free	0.26800
Structure solution method	MAD, MOLECULAR REPLACEMENT
Starting model (for MR)	1G59 Chain A
RMSD bond length	0.013
RMSD bond angle	1.427
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.351	47.400	2.420
High resolution limit [Å]	2.340	5.020	2.340
Rmerge	0.165	0.012	0.012
Number of reflections	35284
<I/σ(I)>	6.6	14.9	1.6
Completeness [%]	99.9	99.6	100
Redundancy		6.57	7.26

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP, NANODROP	8	277	0.2M CaAcetate, 10.0% PEG-8000, 0.1M Imidazole pH 8.0, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K