3BPJ

Crystal structure of human translation initiation factor 3, subunit 1 alpha

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2007-12-17
Detector	RIGAKU RAXIS
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	60.902, 62.373, 88.056
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 1.850
R-factor	0.23
Rwork	0.229
R-free	0.26300
Structure solution method	SIRAS
RMSD bond length	0.016
RMSD bond angle	1.339
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELX
Refinement software	REFMAC (5.3.0037)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.000	30.000	1.920
High resolution limit [Å]	1.850	3.980	1.850
Rmerge	0.041	0.035	0.877
Number of reflections	29322
<I/σ(I)>	24.6
Completeness [%]	99.7	98.1	100
Redundancy	7.3	6.9	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	291	25% PEG 3350, 0.1M Sodium acetate. Chymotrypsin was added to the crystallization sample at a molar ratio of approx. 1:100, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
1	VAPOR DIFFUSION, SITTING DROP	4.5	291	25% PEG 3350, 0.1M Sodium acetate. Chymotrypsin was added to the crystallization sample at a molar ratio of approx. 1:100, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K