8RAI
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis point mutant R90I complexed with phenylhydrazine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-03-02 |
Detector | RIGAKU HyPix-6000HE |
Wavelength(s) | 1.54184 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 85.749, 72.750, 52.341 |
Unit cell angles | 90.00, 100.77, 90.00 |
Refinement procedure
Resolution | 20.820 - 2.000 |
R-factor | 0.15801 |
Rwork | 0.156 |
R-free | 0.19626 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.684 |
Data reduction software | CrysalisPro |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.820 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 | 0.281 |
Rmeas | 0.066 | 0.304 |
Rpim | 0.026 | 0.117 |
Total number of observations | 141122 | 10310 |
Number of reflections | 21415 | 1528 |
<I/σ(I)> | 23 | 7.1 |
Completeness [%] | 99.7 | |
Redundancy | 6.6 | 6.7 |
CC(1/2) | 0.999 | 0.962 |
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 |