1GHE

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	115
Detector technology	CCD
Collection date	2000-09-01
Detector	SBC-2
Spacegroup name	C 1 2 1
Unit cell lengths	101.760, 45.700, 84.240
Unit cell angles	90.00, 105.79, 90.00

Refinement procedure

Resolution	30.000 - 1.550
Rwork	0.209
R-free	0.23000
RMSD bond length	0.198 *
RMSD bond angle	2.400 *
Data reduction software	DENZO (2000)
Data scaling software	SCALEPACK (2000)
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	100.000	1.450
High resolution limit [Å]	1.490 *	1.400
Rmerge	0.071 *	0.320
Total number of observations	307917 *
Number of reflections	56060 *
<I/σ(I)>	5.9
Completeness [%]	92.0 *	65
Redundancy	3	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8	291	PEG 4000, sodium acetate, Tris-HCL, pH 8.0, HANGING DROP/VAPOR DIFFUSION, temperature 291.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	25 (mM)	pH8.0
2	1	drop		150 (mM)
3	1	drop	dithiothreitol	5 (mM)
4	1	drop	PMSF	1 (mM)
5	1	drop	sodium-EDTA	0.2 (mM)
6	1	drop	protein	20-25 (mg/ml)
7	1	reservoir	Tris-HCl	100 (mM)	pH8.0
8	1	reservoir	PEG4000	36 (%(w/v))
9	1	reservoir		0.21 (M)