8YRV
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis complexed with 3-aminooxypropionic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | KURCHATOV SNC BEAMLINE K4.4 |
| Synchrotron site | KURCHATOV SNC |
| Beamline | K4.4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2022-06-03 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.74503 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 86.772, 71.232, 52.549 |
| Unit cell angles | 90.00, 101.26, 90.00 |
Refinement procedure
| Resolution | 35.340 - 1.700 |
| R-factor | 0.16793 |
| Rwork | 0.166 |
| R-free | 0.21040 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.672 |
| Data reduction software | DIALS |
| Data scaling software | Aimless (0.7.8) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.340 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.083 | 0.484 |
| Rmeas | 0.100 | 0.578 |
| Rpim | 0.054 | 0.312 |
| Total number of observations | 107399 | 6072 |
| Number of reflections | 32789 | 1795 |
| <I/σ(I)> | 11.4 | 1.9 |
| Completeness [%] | 94.9 | |
| Redundancy | 3.3 | 3.4 |
| CC(1/2) | 0.991 | 0.602 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.2M MgCl2, 0.1M Bis-tris pH 5.5, 25% PEG 3350, 6mM PLP, 12mM 3-aminooxypropionic acid |
