1KL9

Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F2
Synchrotron site	CHESS
Beamline	F2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-12-27
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9795, 0.9793, 0.9640
Spacegroup name	P 2 2 21
Unit cell lengths	37.280, 44.200, 121.420
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 1.900
R-factor	0.19969
Rwork	0.198
R-free	0.23264
Structure solution method	MAD
RMSD bond length	0.011 *
RMSD bond angle	1.190 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHARP
Refinement software	REFMAC

Data quality characteristics

	Overall
Low resolution limit [Å]	30.000 *
High resolution limit [Å]	1.900
Rmerge	0.060
Number of reflections	14922
<I/σ(I)>	7.7
Completeness [%]	90.9
Redundancy	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	22 *	PEG 4000, sodium acetate, zinc chloride, pH 5.5, VAPOR DIFFUSION, SITTING DROP at 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	30 (mg/ml)
2	1	reservoir	PEG4000	10-16 (%)
3	1	reservoir	sodium acetate	100 (mM)
4	1	reservoir		0.2 (M)