9NH9
Crystal Structure of N-oxygenase HrmI with the diferric cofactor and the N(6)-hydroxy-L-lysine product bound
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2024-03-22 |
Detector | DECTRIS EIGER R 4M |
Wavelength(s) | 1.54184 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 112.520, 112.520, 67.315 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 17.500 - 1.960 |
R-factor | 0.1815 |
Rwork | 0.180 |
R-free | 0.21160 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.905 |
Data reduction software | CrysalisPro |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 17.760 | 2.030 |
High resolution limit [Å] | 1.960 | 1.960 |
Number of reflections | 35485 | 3508 |
<I/σ(I)> | 8.95 | 1.79 |
Completeness [%] | 99.6 | 99.91 |
Redundancy | 10.3 | 10.3 |
CC(1/2) | 0.996 | 0.840 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | Ammonium sulfate and HEPES pH 7.5 |