1AHV

STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 2-NITRO-P-CRESOL

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1996-11
Detector	MARRESEARCH
Spacegroup name	I 4
Unit cell lengths	140.620, 140.620, 132.510
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	100.000 * - 3.100
R-factor	0.206
Rwork	0.205
R-free	0.24900 *
Structure solution method	DENSITY AVERAGING AND LEAST SQUARES REFINEMENT
RMSD bond length	0.006
RMSD bond angle	17.500 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	CCP4
Refinement software	TNT (5E)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	3.200
High resolution limit [Å]	3.100	3.100
Rmerge	0.062 *	0.274
Total number of observations	43741 *
Number of reflections	21522
<I/σ(I)>	8	3
Completeness [%]	94.7	90.1
Redundancy	7	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.6		FROM 6% PEG4000, 100 MM ACETATE BUFFER PH 4.6

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	6 (%(w/v))
2	1	reservoir	sodium acetate/HCl	0.1 (M)