1AV4

CRYSTAL STRUCTURES OF THE COPPER-CONTAINING AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS IN THE HOLO-AND APO-FORMS: IMPLICATIONS FOR THE BIOGENESIS OF TOPA QUINONE

Experimental procedure

Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-6A
Synchrotron site	Photon Factory
Beamline	BL-6A
Temperature [K]	293
Detector technology	FILM
Collection date	1995-12
Spacegroup name	C 1 2 1
Unit cell lengths	158.650, 64.570, 93.290
Unit cell angles	90.00, 113.49, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.2
Rwork	0.200
R-free	0.24100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oac
RMSD bond length	0.011
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000	2.300
High resolution limit [Å]	2.300	2.200
Rmerge	0.085	0.310
Total number of observations	105840 *
Number of reflections	33778
Completeness [%]	90.1	90
Redundancy	3.13

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.1		pH 8.1

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium salfate	1.3 (M)
2	1	reservoir	Tris-HCl	0.1 (M)	pH8.1