9BGP
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 internal aldimine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SEALED TUBE |
Source details | BRUKER D8 QUEST |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-07-22 |
Detector | Bruker PHOTON II |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 53.110, 53.116, 70.322 |
Unit cell angles | 82.59, 82.56, 74.40 |
Refinement procedure
Resolution | 33.450 - 1.250 |
R-factor | 0.16848 |
Rwork | 0.167 |
R-free | 0.18813 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.007 |
RMSD bond angle | 1.520 |
Data reduction software | SAINT |
Data scaling software | SADABS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.350 |
High resolution limit [Å] | 1.250 | 1.250 |
Number of reflections | 199391 | 39859 |
<I/σ(I)> | 10.7 | 2.8 |
Completeness [%] | 98.6 | 95.6 |
Redundancy | 4.9 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 8-12% (w/v) poly(ethylene glycol) 8000, 200 mM LiCl, and 100 mM Homo-PIPES (pH 5.0) |