6X0K
Structure of dithionite-reduced SidA ornithine hydroxylase with the FAD "in" and complexed with L-ornithine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-07 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979180 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 105.902, 155.044, 146.846 |
| Unit cell angles | 90.00, 91.01, 90.00 |
Refinement procedure
| Resolution | 68.553 - 2.231 |
| R-factor | 0.2332 |
| Rwork | 0.231 |
| R-free | 0.28070 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4b63 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.029 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.14) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 155.040 | 155.040 | 2.260 |
| High resolution limit [Å] | 2.230 | 12.190 | 2.230 |
| Rmerge | 0.209 | 0.056 | 1.400 |
| Rmeas | 0.239 | 0.065 | 1.583 |
| Rpim | 0.113 | 0.033 | 0.727 |
| Total number of observations | 1006051 | 5279 | 37428 |
| Number of reflections | 225621 | 1423 | 8596 |
| <I/σ(I)> | 7.8 | 27.8 | 1 |
| Completeness [%] | 97.6 | 96.9 | 75.2 |
| Redundancy | 4.5 | 3.7 | 4.4 |
| CC(1/2) | 0.986 | 0.992 | 0.399 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 293 | Enzyme stock solution: 8-10 mg/mL SidA in 25 mM HEPES (pH 7.5) and 100 mM NaCl. Crystallization reservoir: 17-21 % PEG-3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate. Cryo-buffer: 15 % PEG-200, 20 % PEG 3350, 0.1 M HEPES (pH 7.5), 0.1 M calcium acetate, 50 mM L-ornithine, and 100 mM sodium dithionite |
