4Y9S

structure of an H300N mutant of potato epoxide hydrolase, StEH1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2008-04-18
Detector	ADSC QUANTUM 4
Wavelength(s)	0.93300
Spacegroup name	P 21 21 21
Unit cell lengths	56.021, 96.036, 121.551
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.360 - 2.000
R-factor	0.14957
Rwork	0.147
R-free	0.19873
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cjp
RMSD bond length	0.018
RMSD bond angle	1.817
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	REFMAC (5.8.0073)
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.360	2.090
High resolution limit [Å]	2.000	2.000
Rmerge	0.080
Number of reflections	45161
<I/σ(I)>	14.7	4.4
Completeness [%]	100.0	100
Redundancy	4.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.5	293	1 UL DROPS OF PROTEIN SOLUTION (7.2 MG/ML, I.E. 0.2 MM, IN 30 MM TRIS-HCL, PH 7.4, 5 MM VALPROMIDE) WERE MIXED WITH 1 UL DROPS OF RESERVOIR SOLUTION (CONTAINING 90 MM NA-HEPES, PH 7.5, 25% PEG 10, 000). Once crystals were obtained they were soaked in mother liquor at pH 3.5 prior to freezing.