5K3I
Crystal structure of Acyl-CoA oxidase-1 in Caenorhabditis elegans complexed with FAD and ATP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9787 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 152.339, 141.501, 154.968 |
| Unit cell angles | 90.00, 116.76, 90.00 |
Refinement procedure
| Resolution | 38.736 - 2.683 |
| R-factor | 0.2176 |
| Rwork | 0.217 |
| R-free | 0.23210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5k3g |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.983 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.736 | 2.780 |
| High resolution limit [Å] | 2.630 | 2.630 |
| Rmerge | 0.140 | 0.610 |
| Number of reflections | 163296 | |
| <I/σ(I)> | 8.4 | 0.7 |
| Completeness [%] | 100.0 | 98.3 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 0.4 M NaCl, 0.1 M HEPES pH 7.4, 18% w/v PEG 8000 and 8% v/v glycerol |
