2P91

Crystal structure of Enoyl-[acyl-carrier-protein] reductase (NADH) from Aquifex aeolicus VF5

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2006-08-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97243
Spacegroup name	P 21 21 21
Unit cell lengths	72.078, 119.019, 119.197
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.169
Rwork	0.167
R-free	0.19700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1JW7
RMSD bond length	0.011
RMSD bond angle	1.161
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.070
High resolution limit [Å]	2.000	4.310	2.000
Rmerge		0.060	0.242
Number of reflections	70158
<I/σ(I)>	10
Completeness [%]	99.9	99.2	100
Redundancy	11.1	10.8	10.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	293	USING 2 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (10.93 mg/ml) AND RESERVOIR SOLUTION CONTAINING 0.1 M Phosphate-citrate (pH 4.2), 40% v/v PEG200, 0.15 M Sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K