4DT6

Co-crystal structure of eIF4E with inhibitor

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	90
Detector technology	CCD
Collection date	2007-02-21
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	38.224, 61.073, 122.439
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	36.491 - 2.600
R-factor	0.19446
Rwork	0.191
R-free	0.26715
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	1.686
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	61.200	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.118	0.439
Number of reflections	8533
<I/σ(I)>	9.1	1.7
Completeness [%]	93.0	89.3
Redundancy	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	The purified protein which contained 100 uM m7-GTP was concentrated to about 7 mg/mL in 20 mM Hepes, pH 7.6, 100 mM KCl, 1mM DTT, and 0.1 mM EDTA for crystallization. The m7-GTP-bound eIF4e protein was crystallized with 1:1 ratio of protein solution to reservoir solution of 17-20% PEG-3350 and 0.1-0.4M Na formate, VAPOR DIFFUSION, SITTING DROP, temperature 293K