2PJP

Structure of the mRNA-binding domain of elongation factor SelB from E.coli 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	2005-11-19
Detector	MAR CCD 165 mm
Wavelength(s)	0.9797
Spacegroup name	C 1 2 1
Unit cell lengths	103.498, 56.515, 48.414
Unit cell angles	90.00, 95.60, 90.00

Refinement procedure

Resolution	51.500 - 2.300
R-factor	0.204
Rwork	0.200
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wsu
RMSD bond length	0.021
RMSD bond angle	2.463
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	51.503	18.330	2.110
High resolution limit [Å]	2.000	6.320	2.000
Rmerge	0.101	0.047	0.940
Total number of observations		1931	6524
Number of reflections	18032
<I/σ(I)>	5	12.6	0.6
Completeness [%]	95.7	92.4	92.8
Redundancy	3.5	3.3	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	298	6.7 mM calcium chloride, 33 mM sodium acetate ,10% 2-methyl-2,4-pentanediol, 0.17M sodium fluoride (final), pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents

ID	crystal ID	solution ID	reagent name	concentration	details
1	1	1	calcium chloride
2	1	1	sodium acetate
3	1	1	2-methyl-2,4-pentanediol
4	1	1	sodium fluoride
5	1	2	calcium chloride
6	1	2	sodium acetate
7	1	2	2-methyl-2,4-pentanediol
8	1	2	sodium fluoride