1PS9

The Crystal Structure and Reaction Mechanism of E. coli 2,4-Dienoyl CoA Reductase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-08-21
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	65.601, 109.227, 110.304
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.200
R-factor	0.205
Rwork	0.203
R-free	0.24400 *
Structure solution method	MAD
RMSD bond length	0.010 *
RMSD bond angle	1.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.260
High resolution limit [Å]	2.200	2.200
Rmerge	0.057	0.249
Total number of observations	898148 *
Number of reflections	42467 *
<I/σ(I)>	30.3	7.8
Completeness [%]	94.8	61.2
Redundancy	21.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	292.5	PEG 5000, sodium acetate, ammonium sulfate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 19.5K
1	VAPOR DIFFUSION, HANGING DROP	6.5	292.5	PEG 5000, sodium acetate, ammonium sulfate, MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 19.5K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000 MME	30 (%)
2	1	reservoir	sodium acetate	0.2 (M)
3	1	reservoir	ammonium sulfate	0.1 (M)
4	1	reservoir	MOPS	0.1 (M)	pH6.5
5	1	drop	PEG5000 MME	18 (%)
6	1	drop	sodium acetate	180 (mM)
7	1	drop	ammonium sulfate	90 (mM)
8	1	drop	MOPS	90 (mM)	pH6.5
9	1	drop	protein	15 (mg/ml)