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 | 0.19323 |
Rwork | 0.191 |
R-free | 0.23153 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5cm0 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.533 |
Data reduction software | DIALS |
Data scaling software | Aimless (0.7.4) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 51.030 | 2.000 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.048 | 0.394 |
Rmeas | 0.059 | 0.476 |
Rpim | 0.033 | 0.265 |
Total number of observations | 65244 | 4556 |
Number of reflections | 22696 | 1541 |
<I/σ(I)> | 10.9 | 2.3 |
Completeness [%] | 97.5 | |
Redundancy | 2.9 | 3 |
CC(1/2) | 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. |