1NWW

Limonene-1,2-epoxide hydrolase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	1999-02-06
Detector	ADSC QUANTUM 4
Wavelength(s)	0.931
Spacegroup name	P 21 21 21
Unit cell lengths	45.548, 47.652, 129.701
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.200
R-factor	0.14822
Rwork	0.147
R-free	0.17200 *
Structure solution method	SAD
Starting model (for MR)	Model from structure solution using SAD on Se-Met labelled protein. SAD data collected at ESRF beamline ID14-1 at 0.934 A wavelength.
RMSD bond length	0.025 *
RMSD bond angle	2.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SnB (V. 2.1)
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	64.600	1.210
High resolution limit [Å]	1.200	1.200
Rmerge	0.063 *	0.272 *
Number of reflections	88916
<I/σ(I)>	28.2	3.5
Completeness [%]	99.7	94.1
Redundancy	4.1	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7 *	4 *	PEG 6000, LiCl, MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12.8 (mg/ml)
2	1	drop	HEPES	10 (mM)	pH7.0
3	1	reservoir	PEG6000	30 (%)
4	1	reservoir		1 (M)
5	1	reservoir	MES	0.1 (M)	pH6.0