1EQR

CRYSTAL STRUCTURE OF FREE ASPARTYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-03-27
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	117.749, 161.958, 131.599
Unit cell angles	90.00, 110.36, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.197 *
Rwork	0.198
R-free	0.26900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	E.coli aspartyl-tRNA synthetase - S. cerevisiae tRNA(Asp) complex (Moulinier unpublished)
RMSD bond length	0.011
RMSD bond angle	1.600
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.790
High resolution limit [Å]	2.650	2.650
Rmerge	0.048	0.178
Number of reflections	60472 *	8888 *
<I/σ(I)>	10.3	2.7
Completeness [%]	90.2	92.3
Redundancy	1.76	1.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	288 *	Boeglin, M., (1996) Acta Crystallog. sect., D52, 211. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	PEG6000	5.0 (%)
3	1	drop		530 (mM)
4	1	drop	Bis-Tris	33 (mM)
5	1	reservoir	Bis-Tris	100 (mM)
6	1	reservoir	PEG6000	16 (%)
7	1	reservoir		1.6 (M)