1OAC
CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-06-05 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.89 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 135.732, 167.775, 81.904 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| R-factor | 0.162 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 0.041 |
| Data reduction software | MOSFLM |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.069 |
| Number of reflections | 435398 |
| Completeness [%] | 90.5 |
| Redundancy | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 2.3 (M) | |
| 2 | 1 | reservoir | HEPES | 100 (mM) |
