7P8O
Crystal structure of D-aminoacid transaminase from Haliscomenobacter hydrossis in its intermediate form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-05-05 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 87.636, 72.374, 51.822 |
| Unit cell angles | 90.00, 100.05, 90.00 |
Refinement procedure
| Resolution | 39.870 - 1.950 |
| R-factor | 0.1922 |
| Rwork | 0.190 |
| R-free | 0.23230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5cm0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.513 |
| Data reduction software | DIALS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 51.030 | 51.030 | 2.000 |
| High resolution limit [Å] | 1.950 | 8.930 | 1.950 |
| Rmerge | 0.048 | 0.025 | 0.394 |
| Rmeas | 0.059 | 0.030 | 0.476 |
| Rpim | 0.033 | 0.017 | 0.265 |
| Total number of observations | 65244 | 674 | 4556 |
| Number of reflections | 22696 | 238 | 1541 |
| <I/σ(I)> | 10.9 | 34.9 | 2.3 |
| Completeness [%] | 97.5 | 93.5 | 95.6 |
| Redundancy | 2.9 | 2.8 | 3 |
| CC(1/2) | 0.998 | 0.998 | 0.885 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | MES 0.1 M pH 6.5; MgSO4; 1.8 M NaCl. |
