1QAK

THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-06-21
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	134.660, 166.170, 79.090
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.179
Rwork	0.176
R-free	0.24429
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	1oac
RMSD bond length	0.010
RMSD bond angle	0.043
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.320
High resolution limit [Å]	2.000	2.000
Rmerge	0.067 *	0.164 *
Number of reflections	109845
<I/σ(I)>	8.3	3.2
Completeness [%]	91.4 *	79.2
Redundancy	2.9	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.1		pH 7.1

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium citrate	1.3 (M)
2	1	reservoir	HEPES	100 (mM)