9BGR
X-ray structure of the aminotransferase from Vibrio vulnificus responsible for the biosynthesis of 2,3-diacetamido-4-amino-2,3,4-trideoxy-arabinose in the presence of its external aldimine with 2,3-diacetamido-4-amino-2,3,4-trideoxy-l-arabinose
This is a non-PDB format compatible entry.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER D8 QUEST |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2024-02-23 |
Detector | Bruker PHOTON II |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 52.958, 53.048, 70.267 |
Unit cell angles | 83.00, 82.17, 74.36 |
Refinement procedure
Resolution | 38.960 - 1.050 |
R-factor | 0.16028 |
Rwork | 0.159 |
R-free | 0.17728 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.008 |
RMSD bond angle | 1.663 |
Data reduction software | SAINT |
Data scaling software | SADABS |
Phasing software | REFMAC |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.150 |
High resolution limit [Å] | 1.050 | 1.050 |
Number of reflections | 330200 | 73676 |
<I/σ(I)> | 7.7 | 1.8 |
Completeness [%] | 96.5 | 87.6 |
Redundancy | 4.6 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | protein incubated with 5.0 mM UDP-4-amino-2,3-diacetoamido-2,3,4-trideoxy-L-arabinose and 1.0 mM PLP. Precipitant: 15-20% (w/v) poly(ethylene glycol) 5000, 200 mM NaCl, and 100 mM MES (pH 6.0) |