1DT9

THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA HYDROLYSIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Detector technology	CCD
Spacegroup name	P 43 21 2
Unit cell lengths	77.080, 77.080, 194.440
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
Rwork	0.246
R-free	0.31400
RMSD bond length	0.014
RMSD bond angle	2.000
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	25.000
High resolution limit [Å]	2.700	2.700
Rmerge	0.050	0.406
Total number of observations	82505 *
Number of reflections	16712 *
<I/σ(I)>	8.3
Completeness [%]	99.2	98
Redundancy	4.9	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	20 *	protein was mixed with equal volume of reservoir solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	HEPES	100 (mM)
3	1	reservoir	PEG4000	14-22 (%(w/v))
4	1	reservoir	glycerol	15 (%(v/v))
5	1	reservoir		200 (mM)