1QG6

CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	300
Detector technology	CCD
Collection date	1998-09-01
Detector	ADSC
Spacegroup name	P 1 21 1
Unit cell lengths	74.160, 80.290, 82.750
Unit cell angles	90.00, 104.46, 90.00

Refinement procedure

Resolution	100.000 - 1.900
R-factor	0.201 *
Rwork	0.202
R-free	0.20700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dfh
RMSD bond length	0.012
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	X-PLOR (98.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.450	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.099	0.406
Total number of observations	92854 *
Number of reflections	57294	4320 *
<I/σ(I)>	4.2	1.2
Completeness [%]	78.2 *	40.6 *
Redundancy	1.6	1.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5		HANGING DROPS WERE FORMED BY MIXING 4MICROLITRES OF COMPLEX SOLUTION (15MG/ML PROTEIN, 3MM NADH, 0.6MM TRICLOSAN) WITH 4 MICROLITRES OF A RESERVOIR SOLUTION CONTAINING 12-16% (W/V) PEG 400 AND 0.1M SODIUM ACETATE PH 4.8-5.2 AT ROOM TEMPERATURE, pH 5.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	NADH	3 (mM)
3	1	drop	triclosan	0.6 (mM)
4	1	reservoir	PEG400	12-16 (%(w/v))
5	1	reservoir	sodium acetate	0.1 (M)