5MBX

Crystal structure of reduced murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-10-03
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.975
Spacegroup name	P 61
Unit cell lengths	121.990, 121.990, 54.910
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.810 - 1.400
R-factor	0.181
Rwork	0.180
R-free	0.20000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5lae
RMSD bond length	0.010
RMSD bond angle	1.030
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	BUSTER (2.11.6)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.810	1.480
High resolution limit [Å]	1.400	1.400
Rmerge		0.417
Number of reflections	81328
<I/σ(I)>	20.1	4.5
Completeness [%]	88.8	51.5
Redundancy	10.1	8.4
CC(1/2)		0.908

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	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. N1-ACETYL SPERMINE WAS SOAKED INTO PRE-FORMED CRYSTAL