2PLY

Structure of the mRNA binding fragment of elongation factor SelB in complex with SECIS RNA.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2003-02-20
Detector	MAR CCD 165 mm
Wavelength(s)	0.9797
Spacegroup name	C 1 2 1
Unit cell lengths	158.640, 120.838, 50.865
Unit cell angles	90.00, 100.18, 90.00

Refinement procedure

Resolution	95.350 - 2.600
R-factor	0.22978
Rwork	0.227
R-free	0.28691
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wsu 1lva
RMSD bond length	0.019
RMSD bond angle	2.237
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	95.563	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.115	0.517
Number of reflections	28977
<I/σ(I)>	6	1.3
Completeness [%]	99.7	100
Redundancy	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	294	25% PEG4000, 0.1M Na-Acetate pH 4.6, 0.2M Ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	1	PEG4000
2	1	1	Na-Acetate
3	1	1	Ammonium sulfate
4	1	2	PEG4000
5	1	2	Na-Acetate
6	1	2	Ammonium sulfate