2V9Z

Structure of the Rhodococcus haloalkane dehalogenase mutant with enhanced enantioselectivity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR591
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	2007-04-21
Spacegroup name	P 21 21 21
Unit cell lengths	52.739, 68.900, 84.695
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	53.450 - 3.000
R-factor	0.203
Rwork	0.195
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bn6
RMSD bond length	0.010
RMSD bond angle	1.601
Data reduction software	MOSFLM
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	53.450	3.080
High resolution limit [Å]	3.000	3.000
Rmerge	0.140	0.430
Number of reflections	6389
<I/σ(I)>	8.2	2.3
Completeness [%]	97.9	92.5
Redundancy	3.4	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		281	1 UL OF PROTEIN (5 MG/ML IN 25 MM TRIS-HCL PH 7.5, 150 MM AMMONIUM SULPHATE, 1 MM EDTA) WAS MIXED 1:1 WITH THE RESERVOIR (1 ML) CONSISTED OF 20 % PEG 6000, 0.1 M SODIUM ACETATE, 0.2 M AMMONIUM SULPHATE, 0.1 M TRIS-HCL PH 8.5-9.0. SITTING-DROP 281K.