7P7X
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis (holo 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 | 2021-02-08 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.9677 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 86.884, 71.752, 52.992 |
| Unit cell angles | 90.00, 100.96, 90.00 |
Refinement procedure
| Resolution | 52.030 - 2.000 |
| R-factor | 0.1831 |
| Rwork | 0.180 |
| R-free | 0.24370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5e25 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.949 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (7.1.013) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 52.030 | 52.030 | 1.780 |
| High resolution limit [Å] | 1.750 | 9.090 | 1.750 |
| Rmerge | 0.130 | 0.053 | 1.492 |
| Rmeas | 0.157 | 0.063 | 1.800 |
| Rpim | 0.087 | 0.034 | 0.992 |
| Total number of observations | 96630 | 692 | 5370 |
| Number of reflections | 31622 | 236 | 1726 |
| <I/σ(I)> | 3.8 | 9.7 | 0.8 |
| Completeness [%] | 98.1 | 95.8 | 98.6 |
| Redundancy | 3.1 | 2.9 | 3.1 |
| CC(1/2) | 0.986 | 0.988 | 0.447 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.1M Sodium acetate pH 4.8; 18% PEG3350 |
