1F1R

CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM ARTHROBACTER GLOBIFORMIS (NATIVE, NON-CRYO)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	AREA DETECTOR
Collection date	1998-05-01
Detector	SIEMENS HI-STAR
Spacegroup name	C 1 2 1
Unit cell lengths	138.440, 59.150, 102.800
Unit cell angles	90.00, 118.26, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.156
Rwork	0.156
R-free	0.18700
RMSD bond length	0.020
RMSD bond angle	2.000 *
Data reduction software	X-GEN
Data scaling software	X-GEN
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.920
High resolution limit [Å]	1.750 *	1.850
Rmerge	0.054	0.239 *
Number of reflections	60397
<I/σ(I)>	12.2
Completeness [%]	88.7 *	65 *
Redundancy	2.6 *	1.4 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	6.5 *	18 *	Peg 8000, Mg Acetate, Na cacodylate, pH 6.8, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	100 (mg/ml)
2	1	2	PEG8000	6-10 (%)
3	1	2	magnesium acetate	0.2 (M)
4	1	2	sodium cacodylate	100 (mM)	pH6.5