8PNW
Crystal structure of D-amino acid aminotransferase from Blastococcus saxobsidens in holo form with PLP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-02-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.96770 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 105.935, 105.935, 51.324 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 52.970 - 1.700 |
| R-factor | 0.172 |
| Rwork | 0.171 |
| R-free | 0.19246 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.686 |
| Data reduction software | DIALS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 52.970 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.083 | 0.481 |
| Rmeas | 0.098 | 0.586 |
| Rpim | 0.051 | 0.330 |
| Total number of observations | 124016 | 4957 |
| Number of reflections | 35723 | 1760 |
| <I/σ(I)> | 10.1 | 1.3 |
| Completeness [%] | 97.4 | |
| Redundancy | 3.5 | 2.8 |
| CC(1/2) | 0.994 | 0.792 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.1 M Hepes pH 7.5, 4 M NaCl |
