1FL0

CRYSTAL STRUCTURE OF THE EMAP2/RNA-BINDING DOMAIN OF THE P43 PROTEIN FROM HUMAN AMINOACYL-TRNA SYNTHETASE COMPLEX

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	2000-04-25
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	35.954, 59.683, 37.850
Unit cell angles	90.00, 114.83, 90.00

Refinement procedure

Resolution	34.350 - 1.500
R-factor	0.221
Rwork	0.221
R-free	0.22400
Structure solution method	MIRAS
RMSD bond length	0.004
RMSD bond angle	1.500
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.160
High resolution limit [Å]	1.140	1.140
Rmerge	0.062 *	0.157 *
Total number of observations	269210 *
Number of reflections	52816
<I/σ(I)>	22.5	6.4
Completeness [%]	99.9 *	99.1
Redundancy	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291	35% PEG 3000 or 6000, 100mM TRIS pH7.5, 100-300 mM NaCl, 2mM DTE with a protein concentration of 11 mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	11 (mg/ml)
2	1	reservoir	PEG3000	28-35 (%)	or PEG6000
3	1	reservoir	Tris	100 (mM)
4	1	reservoir		100-300 (mM)
5	1	reservoir	dithiothreitol	2 (mM)