1OMS

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, Hamburg
Beamline	BW7A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-28
Detector	MARRESEARCH
Wavelength(s)	0.9797, 0.9404
Spacegroup name	H 3 2
Unit cell lengths	71.644, 71.644, 375.409
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.900 - 2.300
R-factor	0.208
Rwork	0.208
R-free	0.23800
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	22.900 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	SHARP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.059	0.330
Number of reflections	31810 *
<I/σ(I)>	33.3	6.6
Completeness [%]	99.6	100
Redundancy	4.2 *	4.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.6	6 *	PEG 2000 MME, PEG 400, ammonium sulfate, sodium acetate, tris, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 279K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1.5 (mg/ml)
2	1	reservoir	PEG2000 MME	30 (%)
3	1	reservoir	sodium acetate	85 (mM)
4	1	reservoir	Tris-base	100 (mM)
5	1	reservoir	glycerol	15 (%)