8CP2
Structure of Aspartate-N-hydroxylase (FzmM)from Streptomyces sp. V2: complex with NADPH and L-aspartate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-01-27 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.87313 |
| Spacegroup name | H 3 |
| Unit cell lengths | 244.591, 244.591, 128.114 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 122.300 - 2.100 |
| R-factor | 0.18045 |
| Rwork | 0.179 |
| R-free | 0.20207 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.970 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.7) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 122.300 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.186 | 1.800 |
| Rmeas | 0.301 | 2.439 |
| Rpim | 0.093 | 0.736 |
| Total number of observations | 90751 | |
| Number of reflections | 166781 | 8301 |
| <I/σ(I)> | 7.4 | 1.4 |
| Completeness [%] | 100.0 | |
| Redundancy | 10.6 | 10.9 |
| CC(1/2) | 0.993 | 0.473 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 9% PEG 4000, 1.2 M di-Na tartrate |
