1QQ5

STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	1998-04
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	57.050, 83.928, 91.227
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.520
R-factor	0.198 *
Rwork	0.204
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1aq6
RMSD bond length	0.006
RMSD bond angle	21.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.550
High resolution limit [Å]	1.520	1.520
Rmerge	0.064	0.351
Total number of observations	306585 *
Number of reflections	63057
<I/σ(I)>	24.7
Completeness [%]	92.7	81.4
Redundancy	4.9	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7		used to seeding, Ridder, I.S., (1995) Protein Sci., 4, 2619. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.5 (mg/ml)
2	1	drop	PEG8000	15 (%)
3	1	drop	sodium formate	200 (mM)
4	1	drop	Bis-Tris	100 (mM)
5	1	reservoir	PEG8000	20 (%)
6	1	reservoir	sodium formate	200 (mM)
7	1	reservoir	bis-Tris	100 (mM)