1ONI

Crystal structure of a human p14.5, a translational inhibitor reveals different mode of ligand binding near the invariant residues of the Yjgf/UK114 protein family

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-12-06
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	154.158, 154.158, 104.559
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.900
Rwork	0.185
R-free	0.21600
Structure solution method	SAD
RMSD bond length	0.013
RMSD bond angle	1.542
Data scaling software	SCALEPACK
Phasing software	SnB
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.920
High resolution limit [Å]	1.900	1.900
Rmerge	0.081	0.550
Total number of observations	754078 *
Number of reflections	110385
<I/σ(I)>	22.9	2.3
Completeness [%]	98.4	94.4
Redundancy	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	Sodium malonate, sodium benzoate, pH 7.00, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12.8 (mg/ml)
2	1	reservoir	sodium malonate	2 (M)
3	1	reservoir	sodium benzoate	0.3 (M)	pH7.0