1F1X

CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM BREVIBACTERIUM FUSCUM

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	200
Detector technology	CCD
Collection date	1998-02-07
Detector	CUSTOM-MADE
Spacegroup name	I 41
Unit cell lengths	157.100, 157.100, 121.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.600
R-factor	0.168
Rwork	0.168
R-free	0.19500
RMSD bond length	0.023
RMSD bond angle	2.140 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.041 *	0.127 *
Number of reflections	216266
<I/σ(I)>	20
Completeness [%]	92.9 *	79.5 *
Redundancy	2.55 *	1.51 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5	18 *	Peg5000, Mg Acetate, MOPS, Glycerol was add prior to data collection., pH 7.5, Batch crystallization, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	100 (mg/ml)
2	1	reservoir	PEG5000 MME	10-15 (%)
3	1	reservoir	magnesium acetate	0.2 (M)
4	1	reservoir	MOPS	100 (mM)	pH7.5