9HO1
Room temperature structure of Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Fe, 2-oxoglutarate, and hydroxylated Factor X derived peptide fragment, 1.5 s O2 exposure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | FREE ELECTRON LASER |
| Source details | SLAC LCLS BEAMLINE MFX |
| Synchrotron site | SLAC LCLS |
| Beamline | MFX |
| Temperature [K] | 293 |
| Detector technology | CCD |
| Collection date | 2024-06-03 |
| Detector | RAYONIX MX340-HS |
| Wavelength(s) | 1.266025 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.850, 90.545, 124.621 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.960 - 1.850 |
| R-factor | 0.1984 |
| Rwork | 0.198 |
| R-free | 0.22060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.701 |
| Data reduction software | cctbx.xfel |
| Data scaling software | cctbx.xfel.merge |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.21.1-5286) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.960 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Number of reflections | 49970 | 2485 |
| <I/σ(I)> | 5.01 | 0.794 |
| Completeness [%] | 99.9 | 99.68 |
| Redundancy | 43.92 | 10.1 |
| CC(1/2) | 0.977 | 0.373 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7.5 | 278 | 16% PEG3350, 0.1M Bis Tris propane pH 7.5, 0.1 M KSCN |
