8RAF
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis point mutant R90I (holo form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-19 |
| Detector | RIGAKU HyPix-6000HE |
| Wavelength(s) | 1.54184 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 85.392, 72.627, 52.244 |
| Unit cell angles | 90.00, 100.80, 90.00 |
Refinement procedure
| Resolution | 21.770 - 2.000 |
| R-factor | 0.19649 |
| Rwork | 0.194 |
| R-free | 0.23634 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.819 |
| Data reduction software | CrysalisPro |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.770 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.163 | 0.388 |
| Rmeas | 0.177 | 0.431 |
| Rpim | 0.069 | 0.184 |
| Total number of observations | 135237 | 7667 |
| Number of reflections | 21132 | 1470 |
| <I/σ(I)> | 7 | 3.1 |
| Completeness [%] | 99.4 | |
| Redundancy | 6.4 | 5.2 |
| CC(1/2) | 0.989 | 0.920 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 45% (v/v) Tacsimate, 50 mM BISTRIS buffer, pH 7.0 |
