1HA3

ELONGATION FACTOR TU IN COMPLEX WITH aurodox

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	105
Detector technology	CCD
Collection date	2000-09-15
Detector	X-RAY RESEARCH, HAMBURG, GERMANY
Spacegroup name	P 1 21 1
Unit cell lengths	69.000, 101.400, 79.100
Unit cell angles	90.00, 113.60, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.191
Rwork	0.191
R-free	0.22100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1exm
RMSD bond length	0.007
RMSD bond angle	25.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.067 *	0.263 *
Total number of observations	287768 *
Number of reflections	67199	3322 *
<I/σ(I)>	18.2	3.9
Completeness [%]	99.8	98.7
Redundancy	4.3	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	19 *	HANGING DROP METHOD (PROTEIN SOLUTION:WELL 1:1). PROTEIN CONCENTRATION 10 MG/ML. WELL: 50 MM TRIS, 200 MM NAOAC, 23-25% PEG4000, PH 8.0 MOLAR RATIO EF-TU:GDP:AURODOX = 1:1:5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	sodium acetate	20 (mM)
2	1	drop	ammonium sulfate	100 (mM)
3	1	drop		5 (mM)
4	1	drop	GDP	0.020 (mM)
5	1	drop	protein	9-12 (mg/ml)
6	1	reservoir	Tris	50 (mM)
7	1	reservoir	sodium acetate	200 (mM)
8	1	reservoir	PEG4000	23-25 (%)