4OBY

Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	90
Detector technology	CCD
Collection date	2013-05-09
Detector	ADSC QUANTUM 315
Wavelength(s)	0.979
Spacegroup name	C 1 2 1
Unit cell lengths	118.599, 94.136, 62.717
Unit cell angles	90.00, 110.53, 90.00

Refinement procedure

Resolution	35.906 - 2.574
R-factor	0.2049
Rwork	0.201
R-free	0.27800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1BS2 as ensemble 1 and 3GDZ as ensemble 2
RMSD bond length	0.010
RMSD bond angle	1.250
Data reduction software	DENZO
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	PHENIX ((phenix.refine: 1.8.4_1496))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	50.000
High resolution limit [Å]	2.600	2.600
Number of reflections	20541
Completeness [%]	99.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	289	10mg/ml protein sample in 20 mM Tris, pH 7.5, reservior solution - 50mM HEPES (pH 7.2), 100mM sodium acetate, 22% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K