2HQT

Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-12-17
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97925, 0.97945, 0.95375
Spacegroup name	C 1 2 1
Unit cell lengths	222.317, 89.463, 126.792
Unit cell angles	90.00, 99.39, 90.00

Refinement procedure

Resolution	50.000 - 1.900
R-factor	0.21193
Rwork	0.209
R-free	0.26239
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	1.480
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELXCD
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.000
High resolution limit [Å]	1.900	1.900
Number of reflections	187177
<I/σ(I)>	18.5	3.77
Completeness [%]	97.0	96.5
Redundancy	4.3	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	293	35 % PEG3350, 100 mM LiSO4, 50 mM Tris-acetate pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	8	293	35 % PEG3350, 100 mM LiSO4, 50 mM Tris-acetate pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	8	293	35 % PEG3350, 100 mM LiSO4, 50 mM Tris-acetate pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K