9HO2
Room temperature structure of Aspartyl/Asparaginyl beta-hydroxylase (AspH) in complex with Fe, 2-oxoglutarate and Factor X derived peptide fragment, excess Fe removed
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) | 1.265982 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.896, 91.011, 125.154 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.570 - 1.830 |
| R-factor | 0.1941 |
| Rwork | 0.193 |
| R-free | 0.21870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.522 |
| 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] | 23.570 | 1.860 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Number of reflections | 52092 | 2529 |
| <I/σ(I)> | 4.675 | 0.616 |
| Completeness [%] | 99.9 | 99.76 |
| Redundancy | 46.74 | 10.37 |
| CC(1/2) | 0.970 | 0.316 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BATCH MODE | 7.5 | 278 | 16% PEG 3350, 0.1 M Bis Tris propane pH 7.5, 0.1 M KSCN |
