8AHU
Crystal structure of D-amino acid aminotrensferase from Haliscomenobacter hydrossis complexed with D-cycloserine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-07-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 86.902, 71.940, 53.089 |
| Unit cell angles | 90.00, 101.47, 90.00 |
Refinement procedure
| Resolution | 42.580 - 1.410 |
| R-factor | 0.1732 |
| Rwork | 0.172 |
| R-free | 0.20280 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7p7x |
| RMSD bond length | 0.016 |
| RMSD bond angle | 2.006 |
| Data reduction software | DIALS |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 42.580 | 42.580 | 1.430 |
| High resolution limit [Å] | 1.410 | 7.720 | 1.410 |
| Rmerge | 0.079 | 0.033 | 0.433 |
| Rmeas | 0.086 | 0.037 | 0.473 |
| Rpim | 0.034 | 0.015 | 0.188 |
| Total number of observations | 394915 | 2351 | 18244 |
| Number of reflections | 61465 | 392 | 3027 |
| <I/σ(I)> | 6.5 | 23.6 | 0.6 |
| Completeness [%] | 99.7 | 98.6 | 99.9 |
| Redundancy | 6.4 | 6 | 6 |
| CC(1/2) | 0.998 | 0.992 | 0.946 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 288 | 0.1M sodium acetate pH 4.8, 16-22% PEG 3350 |
