1BEE

HALOALKANE DEHALOGENASE MUTANT WITH TRP 175 REPLACED BY TYR

Experimental procedure

Source type	ROTATING ANODE
Source details	ELLIOTT GX-21
Temperature [K]	298
Detector technology	DIFFRACTOMETER
Collection date	1995-05-08
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 21 21 2
Unit cell lengths	95.180, 72.970, 41.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.193
Rwork	0.193
R-free	0.25300
Starting model (for MR)	2had
RMSD bond length	0.007
RMSD bond angle	23.600 *
Data reduction software	MADNES
Data scaling software	BIOMOL
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.000	2.670
High resolution limit [Å]	2.600	2.600
Rmerge	0.081 *	0.277 *
Total number of observations	13050 *
Number of reflections	7742
<I/σ(I)>	9
Completeness [%]	83.0	80.8 *
Redundancy	1.7	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.6		PROTEIN WAS CRYSTALLIZED FROM 50% AMMONIUM SULFATE, 100 MM MES, PH 5.6

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.5 (mg/ml)
2	1	drop	MES	100 (mM)
3	1	reservoir	ammonium sulfate	50 (%)
4	1	reservoir	MES	100 (mM)