5LFO
Crystal structure of murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-04-11 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.072 |
| Spacegroup name | P 61 |
| Unit cell lengths | 122.292, 122.292, 54.862 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.710 - 1.660 |
| R-factor | 0.199 |
| Rwork | 0.198 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5lae |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.000 |
| 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] | 48.710 | 1.720 |
| High resolution limit [Å] | 1.660 | 1.660 |
| Rmerge | 0.098 | 1.460 |
| Number of reflections | 55475 | |
| <I/σ(I)> | 14.5 | 1.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.1 | 10.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 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 |
