1PJH

Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-10
Detector	MARRESEARCH
Wavelength(s)	0.801
Spacegroup name	P 41 21 2
Unit cell lengths	116.243, 116.243, 216.287
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.168
Rwork	0.168
R-free	0.18900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hnu
RMSD bond length	0.011
RMSD bond angle	1.200 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.200
High resolution limit [Å]	2.100	2.100
Rmerge	0.040	0.199
Total number of observations	690091 *
Number of reflections	86026
<I/σ(I)>	28.5	10.5
Completeness [%]	98.9	93.4
Redundancy	8.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2 *	295	ADA/NaOH, magnesium sulphate, ammonium sulphate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.5 (mg/ml)
2	1	drop	potassium phosphate	20 (mM)	pH7.2
3	1	drop		450 (mM)
4	1	drop	EDTA	1 (mM)
5	1	drop	EGTA	1 (mM)
6	1	drop	benzamidine HCl	0.5 (mM)
7	1	reservoir	ADA	0.1 (M)	pH7.0
8	1	reservoir		0.1 (M)
9	1	reservoir	ammonium sulfate	1.7-2.2 (M)