1E8H

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

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	130.340, 130.340, 134.000
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.600
R-factor	0.237
Rwork	0.237
R-free	0.30300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qlt
RMSD bond length	0.011
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	2.700
High resolution limit [Å]	2.600	2.600
Rmerge	0.090	0.393
Total number of observations	85638 *
Number of reflections	34320
<I/σ(I)>	6	2.8
Completeness [%]	99.8	100
Redundancy	2.5	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.1 *		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	4 (%(w/v))
2	1	reservoir	sodium acetate/HCl	100 (mM)