1E8F

STRUCTURE OF THE H61T MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN THE APO FORM

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	IMAGE PLATE
Collection date	1999-02-15
Detector	MARRESEARCH
Spacegroup name	I 4
Unit cell lengths	129.280, 129.280, 130.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.900
R-factor	0.239
Rwork	0.239
R-free	0.31200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qlt
RMSD bond length	0.012
RMSD bond angle	0.020
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.900
High resolution limit [Å]	2.900	2.800
Rmerge	0.135	0.493
Total number of observations	54479 *
Number of reflections	23727
<I/σ(I)>	6	2.8
Completeness [%]	98.1	98.1
Redundancy	2.3	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.1 *		FROM 100 MM ACETATE BUFFER PH 4.6, 6% PEG4000

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	4 (%(w/v))
2	1	reservoir	sodium acetate/HCl	100 (mM)