5LAE

Crystal structure of murine N1-acetylpolyamine oxidase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2015-01-26
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.972
Spacegroup name	P 61
Unit cell lengths	121.975, 121.975, 55.093
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.000 - 1.850
R-factor	0.181
Rwork	0.179
R-free	0.21000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bq5
RMSD bond length	0.009
RMSD bond angle	0.960
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	BUSTER (2.11.6)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.000	1.890
High resolution limit [Å]	1.850	1.850
Rmerge	0.109	0.870
Number of reflections	40245
<I/σ(I)>	14.9	1.9
Completeness [%]	99.2	95
Redundancy	9.8	6.5
CC(1/2)	0.999

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	293	Protein at 23mg/ml in 20 mM HEPES, pH 7.0, 100 mM NaCl, 5% (v/v) glycerol and 2.5 mM TCEP was equilibrated against 2.2 M (NH4)2SO4, 0.2 M NaSCN, 0.1 M Tris pH 8